메뉴 건너뛰기




Volumn 10, Issue 6, 2013, Pages

The role of focal adhesion kinase in the regulation of cellular mechanical properties

Author keywords

[No Author keywords available]

Indexed keywords

FOCAL ADHESION KINASE; VINCULIN;

EID: 84891435706     PISSN: 14783967     EISSN: 14783975     Source Type: Journal    
DOI: 10.1088/1478-3975/10/6/065005     Document Type: Review
Times cited : (49)

References (287)
  • 4
    • 78650552589 scopus 로고    scopus 로고
    • Forcing form and function: Biomechanical regulation of tumor evolution
    • 10.1016/j.tcb.2010.08.015
    • Yu H, Mouw J K and Weaver V M 2011 Forcing form and function: biomechanical regulation of tumor evolution Trends Cell Biol. 21 47-56
    • (2011) Trends Cell Biol. , vol.21 , pp. 47-56
    • Yu, H.1    Mouw, J.K.2    Weaver, V.M.3
  • 5
    • 79551530752 scopus 로고    scopus 로고
    • Integrin α5β1 facilitates cancer cell invasion through enhanced contractile forces
    • 10.1242/jcs.071985
    • Mierke C T, Frey B, Fellner M, Herrmann M and Fabry B 2011 Integrin α5β1 facilitates cancer cell invasion through enhanced contractile forces J. Cell Sci. 124 369-83
    • (2011) J. Cell Sci. , vol.124 , pp. 369-383
    • Mierke, C.T.1    Frey, B.2    Fellner, M.3    Herrmann, M.4    Fabry, B.5
  • 6
    • 0035948579 scopus 로고    scopus 로고
    • Biochemical signals and biological responses elicited by the focal adhesion kinase
    • DOI 10.1016/S0167-4889(01)00123-9, PII S0167488901001239
    • Schaller M D 2001 Biochemical signals and biological responses elicited by the focal adhesion kinase Biochim. Biophys. Acta 1540 1-21 (Pubitemid 32710044)
    • (2001) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1540 , Issue.1 , pp. 1-21
    • Schaller, M.D.1
  • 7
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: Correlation with preinvasive and invasive phenotypes
    • Cance W G, Harris J E, Iacocca M V, Roche E, Yang X, Chang J, Simkins S and Xu L 2000 Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes Clin. Cancer Res. 6 2417-23 (Pubitemid 30399210)
    • (2000) Clinical Cancer Research , vol.6 , Issue.6 , pp. 2417-2423
    • Cance, W.G.1    Harris, J.E.2    Iacocca, M.V.3    Roche, E.4    Yang, X.H.5    Chang, J.6    Simkins, S.7    Xu, L.H.8
  • 8
    • 9644275426 scopus 로고    scopus 로고
    • Upregulation of focal adhesion kinase (FAK) expression in ductal carcinoma in situ (DCIS) is an early event in breast tumorigenesis
    • DOI 10.1007/s10549-004-1022-8
    • Lightfoot H M Jr, Lark A, Livasy C A, Moore D T, Cowan D, Dressler L, Craven R J and Cance W G 2004 Upregulation of focal adhesion kinase (FAK) expression in ductal carcinoma in situ (DCIS) is an early event in breast tumorigenesis Breast Cancer Res. Treat. 88 109-16 (Pubitemid 39575569)
    • (2004) Breast Cancer Research and Treatment , vol.88 , Issue.2 , pp. 109-116
    • Lightfoot, H.M.1    Lark, A.2    Livasy, C.A.3    Moore, D.T.4    Cowan, D.5    Dressler, L.6    Craven, R.J.7    Cance, W.G.8
  • 9
    • 0037343388 scopus 로고    scopus 로고
    • Focal adhesion kinase as a marker of malignant phenotype in breast and cervical carcinomas
    • DOI 10.1053/hupa.2003.40
    • Oktay M H, Oktay K, Hamele-Bena D, Buyuk A and Koss L G 2003 Focal adhesion kinase as a marker of malignant phenotype in breast and cervical carcinomas Hum. Pathol. 34 240-5 (Pubitemid 36356676)
    • (2003) Human Pathology , vol.34 , Issue.3 , pp. 240-245
    • Oktay, M.H.1    Oktay, K.2    Hamele-Bena, D.3    Buyuk, A.4    Koss, L.G.5
  • 10
    • 0032125580 scopus 로고    scopus 로고
    • Increased levels of phosphatidylinositol 3-kinase activity in colorectal tumors
    • DOI 10.1002/(SICI)1097-0142(19980701)83:1<41::AID-CNCR6>3.0.CO;2-H
    • Phillips W A, St Clair F, Munday A D, Thomas R J and Mitchell C A 1998 Increased levels of phosphatidylinositol 3-kinase activity in colorectal tumors Cancer 83 41-7 (Pubitemid 28299627)
    • (1998) Cancer , vol.83 , Issue.1 , pp. 41-47
    • Phillips, W.A.1    St. Clair, F.2    Munday, A.D.3    Thomas, R.J.S.4    Mitchell, C.A.5
  • 13
    • 34548316989 scopus 로고    scopus 로고
    • Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex
    • DOI 10.1038/ncb1626, PII NCB1626
    • Serrels B, Serrels A, Brunton V G, Holt M, McLean G W, Gray C H, Jones G E and Frame M C 2007 Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex Nat. Cell Biol. 9 1046-56 (Pubitemid 47338144)
    • (2007) Nature Cell Biology , vol.9 , Issue.9 , pp. 1046-1056
    • Serrels, B.1    Serrels, A.2    Brunton, V.G.3    Holt, M.4    McLean, G.W.5    Gray, C.H.6    Jones, G.E.7    Frame, M.C.8
  • 14
    • 33646822656 scopus 로고    scopus 로고
    • Integrin α2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signaling: Identification of a novel signaling pathway
    • DOI 10.1074/jbc.M600787200
    • Sawhney R S, Cookson M M, Omar Y, Hauser J and Brattain M G 2006 Integrin α2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signaling: identification of a novel signaling pathway J. Biol. Chem. 281 8497-510 (Pubitemid 43847952)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.13 , pp. 8497-8510
    • Sawhney, R.S.1    Cookson, M.M.2    Omar, Y.3    Hauser, J.4    Brattain, M.G.5
  • 15
    • 84876000745 scopus 로고    scopus 로고
    • Visualizing and manipulating focal adhesion kinase regulation in live cells
    • 10.1074/jbc.M112.421164
    • Ritt M, Guan J L and Sivaramakrishnan S 2013 Visualizing and manipulating focal adhesion kinase regulation in live cells J. Biol. Chem. 288 8875-86
    • (2013) J. Biol. Chem. , vol.288 , pp. 8875-8886
    • Ritt, M.1    Guan, J.L.2    Sivaramakrishnan, S.3
  • 16
    • 2342627918 scopus 로고    scopus 로고
    • Focal adhesion kinase gene silencing promotes anoikis and suppresses metastasis of human pancreatic adenocarcinoma cells
    • DOI 10.1016/j.surg.2003.10.017
    • Duxbury M S, Ito H, Zinner M J, Ashley S W and Whang E E 2004 Focal adhesion kinase gene silencing promotes anoikis and suppresses metastasis of human pancreatic adenocarcinoma cells Surgery 135 555-62 (Pubitemid 38586530)
    • (2004) Surgery , vol.135 , Issue.5 , pp. 555-562
    • Duxbury, M.S.1    Ito, H.2    Zinner, M.J.3    Ashley, S.W.4    Whang, E.E.5
  • 17
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch S M, Vuori K, Ruoslahti E and Chan-Hui P Y 1996 Control of adhesion dependent cell survival by focal adhesion kinase J. Cell Biol. 134 793-9 (Pubitemid 26269148)
    • (1996) Journal of Cell Biology , vol.134 , Issue.3 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.-Y.4
  • 18
    • 0035476836 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor-stimulated signaling promoting the migration of invasive human carcinoma cells
    • Hauck C R, Sieg D J, Hsia D A, Loftus J C, Gaarde W A, Monia B P and Schlaepfer D D 2001 Inhibition of focal adhesion kinase expression or activity disrupts epidermal growth factor stimulated signaling promoting the migration of invasive human carcinoma cells Cancer Res. 61 7079-90 (Pubitemid 32946499)
    • (2001) Cancer Research , vol.61 , Issue.19 , pp. 7079-7090
    • Hauck, C.R.1    Sieg, D.J.2    Hsia, D.A.3    Loftus, J.C.4    Gaarde, W.A.5    Monia, B.P.6    Schlaepfer, D.D.7
  • 22
    • 41149176839 scopus 로고    scopus 로고
    • β1 integrin/Fak/Src signaling in intestinal epithelial crypt cell survival: Integration of complex regulatory mechanisms
    • 10.1007/s10495-008-0192-y
    • Bouchard V et al 2008 β1 integrin/Fak/Src signaling in intestinal epithelial crypt cell survival: integration of complex regulatory mechanisms Apoptosis 13 531-42
    • (2008) Apoptosis , vol.13 , pp. 531-542
    • Bouchard, V.1
  • 24
    • 0029164237 scopus 로고
    • Integrin transmembrane signaling and cytoskeletal control
    • 10.1016/0955-0674(95)80110-3 0955-0674
    • Yamada K M and Miyamoto S 1995 Integrin transmembrane signaling and cytoskeletal control Curr. Opin. Cell Biol. 7 681-9
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 681-689
    • Yamada, K.M.1    Miyamoto, S.2
  • 25
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • DOI 10.1016/S0955-0674(00)00255-6
    • Geiger B and Bershadsky A 2001 Assembly and mechanosensory function of focal contacts Curr. Opin. Cell Biol. 13 584-92 (Pubitemid 32817017)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.5 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 26
    • 79953148385 scopus 로고    scopus 로고
    • Mechanical signaling through the cytoskeleton regulates cell proliferation by coordinated focal adhesion and Rho GTPase signaling
    • 10.1242/jcs.067009
    • Provenzano P P and Keely P J 2011 Mechanical signaling through the cytoskeleton regulates cell proliferation by coordinated focal adhesion and Rho GTPase signaling J. Cell Sci. 124 1195-205
    • (2011) J. Cell Sci. , vol.124 , pp. 1195-1205
    • Provenzano, P.P.1    Keely, P.J.2
  • 27
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • 10.1083/jcb.130.5.1181
    • Schaller M D, Otey C A, Hildebrand J D and Parsons J T 1995 Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains J. Cell Biol. 130 1181-7
    • (1995) J. Cell Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 28
    • 0034658555 scopus 로고    scopus 로고
    • Association of β1 integrin with focal adhesion kinase and paxillin in differentiating schwann cells
    • Chen L M, Bailey D and Fernandez-Valle C 2000 Association of beta 1 integrin with focal adhesion kinase and paxillin in differentiating schwann cells J. Neurosci. 20 3776-84 (Pubitemid 30266239)
    • (2000) Journal of Neuroscience , vol.20 , Issue.10 , pp. 3776-3784
    • Chen, L.-M.1    Bailey, D.2    Fernandez-Valle, C.3
  • 31
    • 0031915021 scopus 로고    scopus 로고
    • Integrin signalling and tyrosine phosphorylation: Just the FAKs?
    • DOI 10.1016/S0962-8924(97)01172-0
    • Schlaepfer D D and Hunter T 1998 Integrin signalling and tyrosine phosphorylation: just the FAKs? Trends Cell Biol. 8 151-7 (Pubitemid 28142262)
    • (1998) Trends in Cell Biology , vol.8 , Issue.4 , pp. 151-157
    • Schlaepfer, D.D.1    Hunter, T.2
  • 32
    • 0033071270 scopus 로고    scopus 로고
    • The Ntermini of FAK and JAKs contain divergent band 4.1 domains
    • 10.1016/S0968-0004(98)01331-0
    • Girault J A, Labesse G, Mornon J P and Callebaut I 1999 The Ntermini of FAK and JAKs contain divergent band 4.1 domains Trends Biochem. Sci. 24 54-7
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 54-57
    • Girault, J.A.1    Labesse, G.2    Mornon, J.P.3    Callebaut, I.4
  • 33
    • 81055148345 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of cortactin by the FAK-Src complex at focal adhesions regulates cell motility
    • 10.1186/1471-2121-12-49 1471-2121
    • Wang W, Liu Y and Liao K 2011 Tyrosine phosphorylation of cortactin by the FAK-Src complex at focal adhesions regulates cell motility BMC Cell Biol. 12 49
    • (2011) BMC Cell Biol. , vol.12 , pp. 49
    • Wang, W.1    Liu, Y.2    Liao, K.3
  • 35
    • 0036118284 scopus 로고    scopus 로고
    • The structural basis of localization and signaling by the focal adhesion targeting domain
    • DOI 10.1016/S0969-2126(02)00717-7, PII S0969212602007177
    • Arold S T, Hoellerer M K and Noble M E M 2002 The structural basis of localization and signaling by the focal adhesion targeting domain Structure 10 319-27 (Pubitemid 34230620)
    • (2002) Structure , vol.10 , Issue.3 , pp. 319-327
    • Arold, S.T.1    Hoellerer, M.K.2    Noble, M.E.M.3
  • 36
    • 1542289014 scopus 로고    scopus 로고
    • NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: Evidence for a two-site binding model
    • DOI 10.1074/jbc.M309808200
    • Gao G, Prutzman K C, King M L, Scheswohl D M, DeRose E F, London R E, Schaller M D and Campbell S L 2004 NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model J. Biol. Chem. 279 8441-51 (Pubitemid 38294737)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 8441-8451
    • Gao, G.1    Prutzman, K.C.2    King, M.L.3    Scheswohl, D.M.4    DeRose, E.F.5    London, R.E.6    Schaller, M.D.7    Campbell, S.L.8
  • 37
    • 0036172186 scopus 로고    scopus 로고
    • The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
    • DOI 10.1038/nsb755
    • Hayashi I, Vuori K and Liddington R C 2002 The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin Nat. Struct. Biol. 9 101-6 (Pubitemid 34132410)
    • (2002) Nature Structural Biology , vol.9 , Issue.2 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 38
    • 0141483200 scopus 로고    scopus 로고
    • Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain
    • DOI 10.1016/j.str.2003.08.010
    • Hoellerer M K, Noble M E M, Labesse G, Campbell I D, Werner J M and Arold S T 2003 Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain Structure 11 1207-17 (Pubitemid 37214883)
    • (2003) Structure , vol.11 , Issue.10 , pp. 1207-1217
    • Hoellerer, M.K.1    Noble, M.E.M.2    Labesse, G.3    Campbell, I.D.4    Werner, J.M.5    Arold, S.T.6
  • 39
    • 0036197382 scopus 로고    scopus 로고
    • Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase
    • DOI 10.1128/MCB.22.8.2751-2760.2002
    • Liu G, Guibao C D and Zheng J 2002 Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase Mol. Cell. Biol. 22 2751-60 (Pubitemid 34262995)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.8 , pp. 2751-2760
    • Liu, G.1    Guibao, C.D.2    Zheng, J.3
  • 41
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • Owen J D, Ruest P J, Fry D W and Hanks S K 1999 Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2 Mol. Cell. Biol. 19 4806-18 (Pubitemid 29289519)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.7 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2    Fry, D.W.3    Hanks, S.K.4
  • 42
    • 0032820782 scopus 로고    scopus 로고
    • Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration
    • Sieg D J, Hauck C R and Schlaepfer D D 1999 Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration J. Cell Sci. 112 2677-91 (Pubitemid 29429791)
    • (1999) Journal of Cell Science , vol.112 , Issue.16 , pp. 2677-2691
    • Sieg, D.J.1    Hauck, C.R.2    Schlaepfer, D.D.3
  • 43
    • 84876329949 scopus 로고    scopus 로고
    • Akt1 promotes focal adhesion disassembly and cell motility through phosphorylation of FAK in growth factor-stimulated cells
    • 10.1242/jcs.112722
    • Higuchi M, Kihara R, Okazaki T, Aoki I, Suetsugu S and Gotoh Y 2012 Akt1 promotes focal adhesion disassembly and cell motility through phosphorylation of FAK in growth factor-stimulated cells J. Cell Sci. 126 745-55
    • (2012) J. Cell Sci. , vol.126 , pp. 745-755
    • Higuchi, M.1    Kihara, R.2    Okazaki, T.3    Aoki, I.4    Suetsugu, S.5    Gotoh, Y.6
  • 45
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • DOI 10.1016/S0960-9822(00)00537-6
    • Arthur W T, Petch L A and Burridge K 2000 Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism Curr. Biol. 10 719-22 (Pubitemid 30437944)
    • (2000) Current Biology , vol.10 , Issue.12 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 46
    • 0037072731 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells
    • 10.1074/jbc.M204429200
    • Chen B H, Tzen J T, Bresnick A R and Chen H C 2002 Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells J. Biol. Chem. 277 33857-63
    • (2002) J. Biol. Chem. , vol.277 , pp. 33857-33863
    • Chen, B.H.1    Tzen, J.T.2    Bresnick, A.R.3    Chen, H.C.4
  • 48
    • 0031657454 scopus 로고    scopus 로고
    • Focal adhesion kinase and its potential involvement in tumor invasion and metastasis
    • DOI 10.1002/(SICI)1097-0347(199812)20:8<745::AID-HED14>3.0.CO;2-Z
    • Kornberg L J 1998 Focal adhesion kinase and its potential involvement in tumor invasion and metastasis Head Neck 20 745-52 (Pubitemid 28462832)
    • (1998) Head and Neck , vol.20 , Issue.8 , pp. 745-752
    • Kornberg, L.J.1
  • 49
    • 0035947714 scopus 로고    scopus 로고
    • The v-Src SH3 domain facilitates a cell adhesion-independent association with focal adhesion kinase
    • 10.1074/jbc.M009329200
    • Hauck C R, Hunter T and Schlaepfer D D 2001 The v-Src SH3 domain facilitates a cell adhesion-independent association with focal adhesion kinase J. Biol. Chem. 276 17653-62
    • (2001) J. Biol. Chem. , vol.276 , pp. 17653-17662
    • Hauck, C.R.1    Hunter, T.2    Schlaepfer, D.D.3
  • 50
    • 0035826165 scopus 로고    scopus 로고
    • Alterations in the focal adhesion kinase/Src signal transduction pathway correlate with increased migratory capacity of prostate carcinoma cells
    • DOI 10.1038/sj.onc.1204208
    • Slack J K, Adams R B, Rovin J D, Bissonette E A, Stoker C E and Parsons J T 2001 Alterations in the focal adhesion kinase/Src signal transduction pathway correlate with increased migratory capacity of prostate carcinoma cells Oncogene 20 1152-63 (Pubitemid 32226241)
    • (2001) Oncogene , vol.20 , Issue.10 , pp. 1152-1163
    • Slack, J.K.1    Adams, R.B.2    Rovin, J.D.3    Bissonette, E.A.4    Stoker, C.E.5    Parsons, J.T.6
  • 51
    • 0028903083 scopus 로고
    • Augmentation of metalloproteinase (gelatinase) activity secreted from rous sarcoma virus-infected cells correlates with transforming activity of Src
    • 0950-9232
    • Hamaguchi M, Yamagata S, Thant AA, Xiao H, Iwata H, Mazaki T and Hanafusa H 1995 Augmentation of metalloproteinase (gelatinase) activity secreted from rous sarcoma virus-infected cells correlates with transforming activity of Src Oncogene 10 1037-43
    • (1995) Oncogene , vol.10 , pp. 1037-1043
    • Hamaguchi, M.1    Yamagata, S.2    Thant, A.A.3    Xiao, H.4    Iwata, H.5    Mazaki, T.6    Hanafusa, H.7
  • 52
    • 0009374793 scopus 로고    scopus 로고
    • RalA requirement for v-Src- and v-Ras-induced tumorigenicity and overproduction of urokinase-type plasminogen activator: Involvement of metalloproteases
    • DOI 10.1038/sj.onc.1202850
    • Aguirre-Ghiso J A, Frankel P, Farias E F, Lu Z, Jiang H, Olsen A, Feig L A, de Kier Joffe E B and Foster D A 1999 RalA requirement for v-Src- and v-Ras-induced tumorigenicity and overproduction of urokinase-type plasminogen activator: involvement of metalloproteases Oncogene 18 4718-25 (Pubitemid 29417747)
    • (1999) Oncogene , vol.18 , Issue.33 , pp. 4718-4725
    • Aguirre-Ghiso, J.A.1    Frankel, P.2    Farias, E.F.3    Lu, Z.4    Jiang, H.5    Olsen, A.6    Feig, L.A.7    Bal De Kier Joffe, E.8    Foster, D.A.9
  • 53
    • 0037066778 scopus 로고    scopus 로고
    • 1 integrin-containing invadopodia promotes cell invasion
    • DOI 10.1074/jbc.C100760200
    • Hauck C R, Hsia D A, Ilic D and Schlaepfer D D 2002 v-Src SH3-enhanced interaction with focal adhesion kinase at beta 1 integrin-containing invadopodia promotes cell invasion J. Biol. Chem. 277 12487-90 (Pubitemid 34952603)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 12487-12490
    • Hauck, C.R.1    Hsia, D.A.2    Ilic, D.3    Schlaepfer, D.D.4
  • 54
    • 0037011055 scopus 로고    scopus 로고
    • FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth
    • DOI 10.1093/emboj/cdf631
    • Hauck C R, Hsia D A, Puente X S, Cheresh D A and Schlaepfer D D 2002 FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth EMBO J. 21 6289-302 (Pubitemid 35448407)
    • (2002) EMBO Journal , vol.21 , Issue.23 , pp. 6289-6302
    • Hauck, C.R.1    Hsia, D.A.2    Puente, X.S.3    Cheresh, D.A.4    Schlaepfer, D.D.5
  • 55
    • 7944233251 scopus 로고    scopus 로고
    • The interplay between Src and integrins in normal and tumor biology
    • DOI 10.1038/sj.onc.1208080
    • Playford M P and Schaller M D 2004 The interplay between Src and integrins in normal and tumor biology Oncogene 23 7928-46 (Pubitemid 39468852)
    • (2004) Oncogene , vol.23 , Issue.48 REV. ISS. 7 , pp. 7928-7946
    • Playford, M.P.1    Schaller, M.D.2
  • 56
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • Hood J D and Cheresh D A 2002 Role of integrins in cell invasion and migration Nat. Rev. Cancer 2 91-100 (Pubitemid 37328796)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 57
    • 0034176764 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional contributors to tumor progression
    • DOI 10.1016/S1357-4310(00)01686-5, PII S1357431000016865
    • McCawley L J and Matrisian L M 2000 Matrix metalloproteinases: multifunctional contributors to tumor progression Mol. Med. Today 6 149-56 (Pubitemid 30171365)
    • (2000) Molecular Medicine Today , vol.6 , Issue.4 , pp. 149-156
    • McCawley, L.J.1    Matrisian, L.M.2
  • 59
    • 84860389234 scopus 로고    scopus 로고
    • Activation of EGFR promotes squamous carcinoma SCC10A cell migration and invasion via inducing EMT-like phenotype change and MMP-9-mediated degradation of E-cadherin
    • 10.1002/jcb.23175
    • Zuo J H et al 2011 Activation of EGFR promotes squamous carcinoma SCC10A cell migration and invasion via inducing EMT-like phenotype change and MMP-9-mediated degradation of E-cadherin J. Cell Biochem. 112 2508-17
    • (2011) J. Cell Biochem. , vol.112 , pp. 2508-2517
    • Zuo, J.H.1
  • 62
    • 0035671094 scopus 로고    scopus 로고
    • FAK regulates tyrosine phosphorylation of CAS, paxillin, and PYK2 in cells expressing v-Src, but is not a critical determinant of v-Src transformation
    • DOI 10.1002/jcb.10025
    • Roy S, Ruest P J and Hanks S K 2002 FAK regulates tyrosine phosphorylation of CAS, paxillin, and PYK2 in cells expressing v-Src, but is not a critical determinant of v-Src transformation J. Cell. Biochem. 84 377-88 (Pubitemid 34033296)
    • (2001) Journal of Cellular Biochemistry , vol.84 , Issue.2 , pp. 377-388
    • Roy, S.1    Ruest, P.J.2    Hanks, S.K.3
  • 64
    • 84863041492 scopus 로고    scopus 로고
    • FAK promotes recruitment of talin to nascent adhesions to control cell motility
    • 10.1083/jcb.201108078
    • Lawson C, Lim S T, Uryu S, Chen X L, Calderwood D A and Schlaepfer D D 2012 FAK promotes recruitment of talin to nascent adhesions to control cell motility J. Cell Biol. 196 223-32
    • (2012) J. Cell Biol. , vol.196 , pp. 223-232
    • Lawson, C.1    Lim, S.T.2    Uryu, S.3    Chen, X.L.4    Calderwood, D.A.5    Schlaepfer, D.D.6
  • 65
    • 0038048222 scopus 로고    scopus 로고
    • FAK regulates biological processes important for the pathogenesis of cancer
    • DOI 10.1023/A:1023725029589
    • Gabarra-Niecko V, Schaller M D and Dunty J M 2003 FAK regulates biological processes important for the pathogenesis of cancer Cancer Metastasis Rev. 22 359-74 (Pubitemid 36791892)
    • (2003) Cancer and Metastasis Reviews , vol.22 , Issue.4 , pp. 359-374
    • Gabarra-Niecko, V.1    Schaller, M.D.2    Dunty, J.M.3
  • 67
    • 33745186178 scopus 로고    scopus 로고
    • The signaling and biological implications of FAK overexpression in cancer
    • 10.1158/1078-0432.CCR-06-0456 1078-0432
    • Siesser P M and Hanks S K 2006 The signaling and biological implications of FAK overexpression in cancer Clin. Cancer Res. 12 3233-7
    • (2006) Clin. Cancer Res. , vol.12 , pp. 3233-3237
    • Siesser, P.M.1    Hanks, S.K.2
  • 68
    • 33846554255 scopus 로고    scopus 로고
    • Focal adhesion kinase: A potential target in cancer therapy
    • DOI 10.1016/j.bcp.2006.08.011, PII S0006295206005053
    • van Nimwegen M J and van de Water B 2007 Focal adhesion kinase: a potential target in cancer therapy Biochem. Pharmacol. 73 597-609 (Pubitemid 46161372)
    • (2007) Biochemical Pharmacology , vol.73 , Issue.5 , pp. 597-609
    • Van Nimwegen, M.J.1    Van De Water, B.2
  • 69
    • 0041426730 scopus 로고    scopus 로고
    • Simultaneous inhibition of focal adhesion kinase and Src enhances detachment and apoptosis in colon cancer cell lines
    • Golubovskaya V M, Gross S, Kaur A S, Wilson R I, Xu L H, Yang X H and Cance W G 2003 Simultaneous inhibition of focal adhesion kinase and SRC enhances detachment and apoptosis in colon cancer cell lines Mol. Cancer Res. 1 755-64 (Pubitemid 37025594)
    • (2003) Molecular Cancer Research , vol.1 , Issue.10 , pp. 755-764
    • Golubovskaya, V.M.1    Gross, S.2    Kaur, A.S.3    Wilson, R.I.4    Xu, L.-H.5    Yang, X.H.6    Cance, W.G.7
  • 70
    • 77955587900 scopus 로고    scopus 로고
    • Focal adhesion kinase is required for intestinal regeneration and tumorigenesis downstream of Wnt/c-Myc signaling
    • 10.1016/j.devcel.2010.07.015 1534-5807
    • Ashton G H et al 2010 Focal adhesion kinase is required for intestinal regeneration and tumorigenesis downstream of Wnt/c-Myc signaling Dev. Cell 19 259-69
    • (2010) Dev. Cell , vol.19 , pp. 259-269
    • Ashton, G.H.1
  • 72
    • 58349108303 scopus 로고    scopus 로고
    • Mammary epithelialspecific ablation of the focal adhesion kinase suppresses mammary tumorigenesis by affecting mammary cancer stem/progenitor cells
    • 10.1158/0008-5472.CAN-08-3078
    • Luo M, Fan H, Nagy T, Wei H, Wang C, Liu S, Wicha M S and Guan J L 2009 Mammary epithelialspecific ablation of the focal adhesion kinase suppresses mammary tumorigenesis by affecting mammary cancer stem/progenitor cells Cancer Res. 69 466-74
    • (2009) Cancer Res. , vol.69 , pp. 466-474
    • Luo, M.1    Fan, H.2    Nagy, T.3    Wei, H.4    Wang, C.5    Liu, S.6    Wicha, M.S.7    Guan, J.L.8
  • 74
    • 55349105491 scopus 로고    scopus 로고
    • Mammary epithelial-specific disruption of focal adhesion kinase retards tumor formation and metastasis in a transgenic mouse model of human breast cancer
    • 10.2353/ajpath.2008.080308
    • Provenzano P P, Inman D R, Eliceiri K W, Beggs H E and Keely P J 2008 Mammary epithelial-specific disruption of focal adhesion kinase retards tumor formation and metastasis in a transgenic mouse model of human breast cancer Am. J. Pathol. 173 1551-65
    • (2008) Am. J. Pathol. , vol.173 , pp. 1551-1565
    • Provenzano, P.P.1    Inman, D.R.2    Eliceiri, K.W.3    Beggs, H.E.4    Keely, P.J.5
  • 75
    • 61749094852 scopus 로고    scopus 로고
    • Ras and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling
    • 0021-9738
    • Pylayeva Y, Gillen K M, Gerald W, Beggs H E, Reichardt L F and Giancotti F G 2009 Ras and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling J. Clin. Invest. 119 252-66
    • (2009) J. Clin. Invest. , vol.119 , pp. 252-266
    • Pylayeva, Y.1    Gillen, K.M.2    Gerald, W.3    Beggs, H.E.4    Reichardt, L.F.5    Giancotti, F.G.6
  • 76
    • 68849114514 scopus 로고    scopus 로고
    • Differential requirement for focal adhesion kinase signaling in cancer progression in the transgenic adenocarcinoma of mouse prostate model
    • 10.1158/1535-7163.MCT-09-0262
    • Slack-Davis J K, Hershey E D, Theodorescu D, Frierson H F and Parsons J T 2009 Differential requirement for focal adhesion kinase signaling in cancer progression in the transgenic adenocarcinoma of mouse prostate model Mol. Cancer Ther. 8 2470-7
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 2470-2477
    • Slack-Davis, J.K.1    Hershey, E.D.2    Theodorescu, D.3    Frierson, H.F.4    Parsons, J.T.5
  • 77
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • DOI 10.1016/j.ceb.2006.08.011, PII S0955067406001220
    • Mitra S K and Schlaepfer D D 2006 Integrin-regulated FAK-Src signaling in normal and cancer cells Curr. Opin. Cell Biol. 18 516-23 (Pubitemid 44332916)
    • (2006) Current Opinion in Cell Biology , vol.18 , Issue.5 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 78
    • 84964872797 scopus 로고    scopus 로고
    • Focal adhesion kinase is a phospho-regulated repressor of Rac and proliferation in human endothelial cells
    • 10.1242/bio.20121008
    • Bryant P W, Zheng Q and Pumiglia K 2012 Focal adhesion kinase is a phospho-regulated repressor of Rac and proliferation in human endothelial cells Biol. Open. 1 723-30
    • (2012) Biol. Open. , vol.1 , pp. 723-730
    • Bryant, P.W.1    Zheng, Q.2    Pumiglia, K.3
  • 80
    • 78649633119 scopus 로고    scopus 로고
    • P53-Dependent repression of focal adhesion kinase in response to estradiol in breast cancer cell-lines
    • 10.1016/j.canlet.2010.10.008
    • Anaganti S, Fernández-Cuesta L, Langerød A, Hainaut P and Olivier M 2011 p53-Dependent repression of focal adhesion kinase in response to estradiol in breast cancer cell-lines Cancer Lett. 300 215-24
    • (2011) Cancer Lett. , vol.300 , pp. 215-224
    • Anaganti, S.1    Fernández-Cuesta, L.2    Langerød, A.3    Hainaut, P.4    Olivier, M.5
  • 84
    • 0032547796 scopus 로고    scopus 로고
    • Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis
    • DOI 10.1083/jcb.143.2.547
    • Ilic D, Almeida E A, Schlaepfer D D, Dazin P, Aizawa S and Damsky C H 1998 Extracellular matrix survival signals transduced by focal adhesion kinase suppress p53-mediated apoptosis J. Cell Biol. 143 547-60 (Pubitemid 28487870)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 547-560
    • Ilic, D.1    Almeida, E.A.C.2    Schlaepfer, D.D.3    Dazin, P.4    Aizawa, S.5    Damsky, C.H.6
  • 85
    • 84866401427 scopus 로고    scopus 로고
    • N-terminal cleavage fragment of focal adhesion kinase is required to activate the survival signalling pathway in cultured myoblasts under oxidative stress
    • 10.1111/j.1742-4658.2012.08715.x 1742-464X
    • Lim J A, Hwang S H, Kim M J, Kim S S and Kim H S 2012 N-terminal cleavage fragment of focal adhesion kinase is required to activate the survival signalling pathway in cultured myoblasts under oxidative stress FEBS J. 279 3573-83
    • (2012) FEBS J. , vol.279 , pp. 3573-3583
    • Lim, J.A.1    Hwang, S.H.2    Kim, M.J.3    Kim, S.S.4    Kim, H.S.5
  • 86
    • 77953709612 scopus 로고    scopus 로고
    • PND-1186 FAK inhibitor selectively promotes tumor cell apoptosis in three-dimensional environments
    • 10.4161/cbt.9.10.11434 1538-4047
    • Tanjoni I et al 2010 PND-1186 FAK inhibitor selectively promotes tumor cell apoptosis in three-dimensional environments Cancer Biol. Ther. 9 764-77
    • (2010) Cancer Biol. Ther. , vol.9 , pp. 764-777
    • Tanjoni, I.1
  • 87
    • 27944509109 scopus 로고    scopus 로고
    • Differential effect of the focal adhesion kinase Y397F mutant on v-Src-stimulated cell invasion and tumor growth
    • DOI 10.1007/s11373-005-7212-5
    • Chang L C, Huang C H, Cheng C H, Chen B H and Chen H C 2005 Differential effect of the focal adhesion kinase Y397F mutant on v-Src-stimulated cell invasion and tumor growth J. Biomed. Sci. 12 571-85 (Pubitemid 41673381)
    • (2005) Journal of Biomedical Science , vol.12 , Issue.4 , pp. 571-585
    • Chang, L.-C.1    Huang, C.-H.2    Cheng, C.-H.3    Chen, B.-H.4    Chen, H.-C.5
  • 88
    • 0030694182 scopus 로고    scopus 로고
    • Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: A role for paxillin tyrosine phosphorylation
    • Richardson A, Malik R K, Hildebrand J D and Parsons J T 1997 Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation Mol. Cell Biol. 17 6906-14 (Pubitemid 27505920)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 6906-6914
    • Richardson, A.1    Malik, R.K.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 89
    • 84867525729 scopus 로고    scopus 로고
    • Focal adhesion kinase activates NF-κB via the ERK1/2 and p38MAPK Pathways in amyloid-β25-35-induced apoptosis in PC12 cells
    • Wang X, Chen Q and Xing D 2012 Focal adhesion kinase activates NF-κB via the ERK1/2 and p38MAPK Pathways in amyloid-β25-35-induced apoptosis in PC12 cells J. Alzheimers Dis. 32 77-94
    • (2012) J. Alzheimers Dis. , vol.32 , pp. 77-94
    • Wang, X.1    Chen, Q.2    Xing, D.3
  • 91
    • 84863773500 scopus 로고    scopus 로고
    • The gain of function of p53 mutant p53S in promoting tumorigenesis by cross-talking with H-RasV12
    • 10.7150/ijbs.4176
    • Jia S, Zhao L, Tang W and Luo Y 2012 The gain of function of p53 mutant p53S in promoting tumorigenesis by cross-talking with H-RasV12 Int. J. Biol. Sci. 8 596-605
    • (2012) Int. J. Biol. Sci. , vol.8 , pp. 596-605
    • Jia, S.1    Zhao, L.2    Tang, W.3    Luo, Y.4
  • 92
    • 16844362817 scopus 로고    scopus 로고
    • Lack of correlation between p53-dependent transcriptional activity and the ability to induce apostosis among 179 mutant p53s
    • DOI 10.1158/0008-5472.CAN-04-2935
    • Kakudo Y, Shibata H, Otsuka K, Kato S and Ishioka C 2005 Lack of correlation between p53-dependent transcriptional activity and the ability to induce apoptosis among 179 mutant p53s Cancer Res. 65 2108-14 (Pubitemid 40490116)
    • (2005) Cancer Research , vol.65 , Issue.6 , pp. 2108-2114
    • Kakudo, Y.1    Shibata, H.2    Otsuka, K.3    Kato, S.4    Ishioka, C.5
  • 95
    • 0034717285 scopus 로고    scopus 로고
    • Anti-apoptotic role of focal adhesion kinase (FAK): Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60
    • DOI 10.1074/jbc.275.21.16309
    • Sonoda Y, Matsumoto Y, Funakoshi M, Yamamoto D, Hanks S K and Kasahara T 2000 Anti-apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor-of-apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL-60 J. Biol. Chem. 275 16309-15 (Pubitemid 30366946)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 16309-16315
    • Sonoda, Y.1    Matsumoto, Y.2    Funakoshi, M.3    Yamamoto, D.4    Hanks, S.K.5    Kasahara, T.6
  • 96
    • 0032547737 scopus 로고    scopus 로고
    • Layilin, a novel talin-binding transmembrane protein homologous with C- type lectins, is localized in membrane ruffles
    • DOI 10.1083/jcb.143.2.429
    • Borowsky M L and Hynes R O 1998 Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles J. Cell Biol. 143 429-42 (Pubitemid 28487861)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 429-442
    • Borowsky, M.L.1    Hynes, R.O.2
  • 97
    • 21644466387 scopus 로고    scopus 로고
    • Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53
    • DOI 10.1074/jbc.M414172200
    • Golubovskaya V M, Finch R and Cance W G 2005 Direct interaction of the N-terminal domain of focal adhesion kinase with the N-terminal transactivation domain of p53 J. Biol. Chem. 280 25008-21 (Pubitemid 40934593)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 25008-25021
    • Golubovskaya, V.M.1    Finch, R.2    Cance, W.G.3
  • 98
    • 0031003706 scopus 로고    scopus 로고
    • 3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation
    • DOI 10.1074/jbc.272.12.7892
    • Tahiliani P D, Singh L, Auer K L and LaFlamme S E 1997 The role of conserved amino acid motifs within the integrin β3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation J. Biol. Chem. 272 7892-8 (Pubitemid 27137349)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.12 , pp. 7892-7898
    • Tahiliani, P.D.1    Singh, L.2    Auer, K.L.3    LaFlamme, S.E.4
  • 99
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • Brown M C, Perrotta J A and Turner C E 1996 Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding J. Cell Biol. 135 1109-23 (Pubitemid 26403782)
    • (1996) Journal of Cell Biology , vol.135 , Issue.4 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 100
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • DOI 10.1016/j.ceb.2007.08.002, PII S0955067407001196, Cell to Cell Contact and Extracellular Matrix
    • Arnaout M A, Goodman S L and Xiong J P 2007 Structure and mechanics of integrin-based cell adhesion Curr. Opin. Cell Biol. 19 495-507 (Pubitemid 350019555)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.-P.3
  • 101
    • 34547106599 scopus 로고    scopus 로고
    • EphrinA1 activates a Src/focal adhesion kinase-mediated motility response leading to rho-dependent actino/myosin contractility
    • DOI 10.1074/jbc.M701319200
    • Parri M, Buricchi F, Giannoni E, Grimaldi G, Mello T, Raugei G, Ramponi G and Chiarugi P 2007 EphrinA1 activates a Src/focal adhesion kinase-mediated motility response leading to Rho-dependent actino/myosin contractility J. Biol. Chem. 282 19619-28 (Pubitemid 47100120)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.27 , pp. 19619-19628
    • Parri, M.1    Buricchi, F.2    Giannoni, E.3    Grimaldi, G.4    Mello, T.5    Raugei, G.6    Ramponi, G.7    Chiarugi, P.8
  • 102
    • 0031257749 scopus 로고    scopus 로고
    • Focal adhesion kinase in integrin signaling
    • DOI 10.1016/S0945-053X(97)90008-1
    • Guan J L 1997 Focal adhesion kinase in integrin signaling Matrix Biol. 16 195-200 (Pubitemid 27487661)
    • (1997) Matrix Biology , vol.16 , Issue.4 , pp. 195-200
    • Guan, J.-L.1
  • 104
    • 84861637416 scopus 로고    scopus 로고
    • The role of focal adhesion kinase catalytic activity on the proliferation and migration of squamous cell carcinoma cells
    • 10.1002/ijc.26351
    • Serrels A, McLeod K, Canel M, Kinnaird A, Graham K, Frame M C and Brunton V G 2012 The role of focal adhesion kinase catalytic activity on the proliferation and migration of squamous cell carcinoma cells Int. J. Cancer 131 287-97
    • (2012) Int. J. Cancer , vol.131 , pp. 287-297
    • Serrels, A.1    McLeod, K.2    Canel, M.3    Kinnaird, A.4    Graham, K.5    Frame, M.C.6    Brunton, V.G.7
  • 105
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • 10.1016/0092-8674(92)90163-7
    • Ridley A J and Hall A 1992 The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors Cell 70 389-99
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 107
    • 0036205320 scopus 로고    scopus 로고
    • Src catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • DOI 10.1128/MCB.22.8.2427-2440.2002
    • Cary L A, Klinghoffer R A, Sachsenmaier C and Cooper J A 2002 SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading Mol. Cell Biol. 22 2427-40 (Pubitemid 34262966)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.8 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 108
    • 0031921101 scopus 로고    scopus 로고
    • Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: Summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events?
    • Schlaepfer D D, Jones K C and Hunter T 1998 Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events Mol. Cell Biol. 18 2571-85 (Pubitemid 28183427)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.5 , pp. 2571-2585
    • Schlaepfer, D.D.1    Jones, K.C.2    Hunter, T.3
  • 109
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase
    • 10.1038/372786a0 0028-0836
    • Schlaepfer D D, Hanks S K, Hunter T and van der Geer P 1994 Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase Nature 372 786-91
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 110
    • 46649092797 scopus 로고    scopus 로고
    • Activation of KLF8 transcription by focal adhesion kinase in human ovarian epithelial and cancer cells
    • 10.1074/jbc.M709300200
    • Wang X, Urvalek A M, Liu J and Zhao J 2008 Activation of KLF8 transcription by focal adhesion kinase in human ovarian epithelial and cancer cells J. Biol. Chem. 283 13934-42
    • (2008) J. Biol. Chem. , vol.283 , pp. 13934-13942
    • Wang, X.1    Urvalek, A.M.2    Liu, J.3    Zhao, J.4
  • 111
    • 33846815130 scopus 로고    scopus 로고
    • Focal adhesion signaling and actin stress fibers are dispensable for progression through the ongoing cell cycle
    • DOI 10.1242/jcs.03301
    • Margadant C, van Opstal A and Boonstra J 2007 Focal adhesion signaling and actin stress fibers are dispensable for progression through the ongoing cell cycle J. Cell Sci. 120 66-76 (Pubitemid 46206650)
    • (2007) Journal of Cell Science , vol.120 , Issue.1 , pp. 66-76
    • Margadant, C.1    Van Opstal, A.2    Boonstra, J.3
  • 112
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • DOI 10.1083/jcb.144.6.1235
    • Nobes C D and Hall A 1999 Rho GTPases control polarity, protrusion, and adhesion during cell movement J. Cell Biol. 144 1235-44 (Pubitemid 29157301)
    • (1999) Journal of Cell Biology , vol.144 , Issue.6 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 113
    • 0030940218 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages
    • Allen W E, Jones G E, Pollard J W and Ridley A J 1997 Rho, Rac and Cdc42 regulate actin organization and cell adhesion in macrophages J. Cell Sci. 110 707-20 (Pubitemid 27156320)
    • (1997) Journal of Cell Science , vol.110 , Issue.6 , pp. 707-720
    • Allen, W.E.1    Jones, G.E.2    Pollard, J.W.3    Ridley, A.J.4
  • 115
    • 84876089304 scopus 로고    scopus 로고
    • E-cadherin-integrin crosstalk in cancer invasion and metastasis
    • 10.1242/jcs.100115
    • Canel M, Serrels A, Frame M C and Brunton V G 2013 E-cadherin-integrin crosstalk in cancer invasion and metastasis J. Cell Sci. 126 393-401
    • (2013) J. Cell Sci. , vol.126 , pp. 393-401
    • Canel, M.1    Serrels, A.2    Frame, M.C.3    Brunton, V.G.4
  • 116
    • 0026476697 scopus 로고
    • Focal adhesion kinase (p125FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes
    • 10.1016/0092-8674(92)90385-P
    • Zachary I and Rozengurt E 1992 Focal adhesion kinase (p125FAK): a point of convergence in the action of neuropeptides, integrins, and oncogenes Cell 71 891-4
    • (1992) Cell , vol.71 , pp. 891-894
    • Zachary, I.1    Rozengurt, E.2
  • 117
    • 0027291705 scopus 로고
    • Focal adhesion kinase: An integrin-linked protein tyrosine kinase
    • DOI 10.1016/0962-8924(93)90053-4
    • Schaller M D and Parsons J T 1993 Focal adhesion kinase: an integrin-linked protein tyrosine kinase Trends Cell Biol. 3 258-62 (Pubitemid 23214974)
    • (1993) Trends in Cell Biology , vol.3 , Issue.8 , pp. 258-262
    • Schaller, M.D.1    Parsons, J.T.2
  • 118
    • 0031917388 scopus 로고    scopus 로고
    • Differential regulation of Pyk2 and focal adhesion kinase (FAK): The C- terminal domain of FAK confers response to cell adhesion
    • DOI 10.1074/jbc.273.4.2384
    • Zheng C, Xing Z, Bian Z C, Guo C, Akbay A, Warner L and Guan J L 1998 Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion J. Biol. Chem. 273 2384-9 (Pubitemid 28069295)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.4 , pp. 2384-2389
    • Zheng, C.1    Xing, Z.2    Bian, Z.C.3    Guo, C.4    Akbay, A.5    Warner, L.6    Guan, J.-L.7
  • 122
    • 84863340961 scopus 로고    scopus 로고
    • In vitro phosphorylation of the focal adhesion targeting domain of focal adhesion kinase by Src kinase
    • 10.1021/bi300123a
    • Cable J, Prutzman K, Gunawardena H P, Schaller M D, Chen X and Campbell S L 2012 In vitro phosphorylation of the focal adhesion targeting domain of focal adhesion kinase by Src kinase Biochemistry 51 2213-23
    • (2012) Biochemistry , vol.51 , pp. 2213-2223
    • Cable, J.1    Prutzman, K.2    Gunawardena, H.P.3    Schaller, M.D.4    Chen, X.5    Campbell, S.L.6
  • 123
    • 79955944293 scopus 로고    scopus 로고
    • Non-Smad transforming growth factor-β signaling regulated by focal adhesion kinase binding the p85 subunit of phosphatidylinositol 3-kinase
    • 10.1074/jbc.M111.233676
    • Hong M, Wilkes M C, Penheiter S G, Gupta S K, Edens M and Leof E B 2011 Non-Smad transforming growth factor-β signaling regulated by focal adhesion kinase binding the p85 subunit of phosphatidylinositol 3-kinase J. Biol. Chem. 286 17841-50
    • (2011) J. Biol. Chem. , vol.286 , pp. 17841-17850
    • Hong, M.1    Wilkes, M.C.2    Penheiter, S.G.3    Gupta, S.K.4    Edens, M.5    Leof, E.B.6
  • 124
    • 0035875975 scopus 로고    scopus 로고
    • Differential regulation of cell migration and cell cycle progression by FAK complexes with Src, PI3K, Grb7 and Grb2 in focal contacts
    • DOI 10.1016/S0014-5793(01)02545-5, PII S0014579301025455
    • Shen T L and Guan J L 2001 Differential regulation of cell migration and cell cycle progression by FAK complexes with Src, PI3K, Grb7 and Grb2 in focal contacts FEBS Lett. 499 176-81 (Pubitemid 32539344)
    • (2001) FEBS Letters , vol.499 , Issue.1-2 , pp. 176-181
    • Shen, T.-L.1    Guan, J.-L.2
  • 125
    • 84891949141 scopus 로고    scopus 로고
    • In vivo cleaved CDCP1 promotes early tumor dissemination via complexing with activated β1 integrin and induction of FAK/PI3K/Akt motility signaling
    • Casar B, Rimann I, Kato H, Shattil S J, Quigley J P and Deryugina E I 2012 In vivo cleaved CDCP1 promotes early tumor dissemination via complexing with activated β1 integrin and induction of FAK/PI3K/Akt motility signaling Oncogene doi:10.1038/onc.2012.547
    • (2012) Oncogene
    • Casar, B.1    Rimann, I.2    Kato, H.3    Shattil, S.J.4    Quigley, J.P.5    Deryugina, E.I.6
  • 126
    • 3543023861 scopus 로고    scopus 로고
    • 1 integrin viability signaling pathway
    • DOI 10.1074/jbc.M313265200
    • Xia H, Nho R S, Kahm J, Kleidon J and Henke C A 2004 Focal adhesion kinase is upstream of phosphatidylinositol 3-kinase/Akt in regulating fibroblast survival in response to contraction of type I collagen matrices via a beta 1 integrin viability signaling pathway J. Biol. Chem. 279 33024-34 (Pubitemid 39014762)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 33024-33034
    • Xia, H.1    Nho, R.S.2    Kahm, J.3    Kleidon, J.4    Henke, C.A.5
  • 127
    • 84855984472 scopus 로고    scopus 로고
    • Focal adhesion kinase governs cardiac concentric hypertrophic growth by activating the Akt and mTOR pathways
    • 10.1016/j.yjmcc.2011.10.015
    • Clemente C F et al 2012 Focal adhesion kinase governs cardiac concentric hypertrophic growth by activating the Akt and mTOR pathways J. Mol. Cell Cardiol. 52 493-501
    • (2012) J. Mol. Cell Cardiol. , vol.52 , pp. 493-501
    • Clemente, C.F.1
  • 128
    • 84855233177 scopus 로고    scopus 로고
    • Fascin, a novel marker of human hepatic stellate cells, may regulate their proliferation, migration, and collagen gene expression through the FAK-PI3K-Akt pathway
    • 10.1038/labinvest.2011.150 0023-6837
    • Uyama N, Iimuro Y, Kawada N, Reynaert H, Suzumura K, Hirano T, Kuroda N and Fujimoto J 2012 Fascin, a novel marker of human hepatic stellate cells, may regulate their proliferation, migration, and collagen gene expression through the FAK-PI3K-Akt pathway Lab. Invest. 92 57-71
    • (2012) Lab. Invest. , vol.92 , pp. 57-71
    • Uyama, N.1    Iimuro, Y.2    Kawada, N.3    Reynaert, H.4    Suzumura, K.5    Hirano, T.6    Kuroda, N.7    Fujimoto, J.8
  • 129
    • 78650902018 scopus 로고    scopus 로고
    • PI3-kinase p110α mediates β1 integrin-induced Akt activation and membrane protrusion during cell attachment and initial spreading
    • 10.1016/j.cellsig.2010.07.011 0898-6568
    • Zeller K S, Idevall-Hagren O, Stefansson A, Velling T, Jackson S P, Downward J, Tengholm A and Johansson S 2010 PI3-kinase p110α mediates β1 integrin-induced Akt activation and membrane protrusion during cell attachment and initial spreading Cell. Signal. 22 1838-48
    • (2010) Cell. Signal. , vol.22 , pp. 1838-1848
    • Zeller, K.S.1    Idevall-Hagren, O.2    Stefansson, A.3    Velling, T.4    Jackson, S.P.5    Downward, J.6    Tengholm, A.7    Johansson, S.8
  • 130
    • 84877115047 scopus 로고    scopus 로고
    • Stiff collagen matrices increase tumorigenic prolactin signaling in breast cancer cells
    • 10.1074/jbc.M112.447631
    • Barcus C E, Keely P J, Eliceiri K W and Schuler L A 2013 Stiff collagen matrices increase tumorigenic prolactin signaling in breast cancer cells J. Biol. Chem. 288 12722-32
    • (2013) J. Biol. Chem. , vol.288 , pp. 12722-12732
    • Barcus, C.E.1    Keely, P.J.2    Eliceiri, K.W.3    Schuler, L.A.4
  • 131
    • 84875874566 scopus 로고    scopus 로고
    • An evaluation of focal adhesion kinase in breast cancer by tissue microarrays
    • 0250-7005
    • Sheen-Chen S M et al 2013 An evaluation of focal adhesion kinase in breast cancer by tissue microarrays Anticancer Res. 33 1169-73
    • (2013) Anticancer Res. , vol.33 , pp. 1169-1173
    • Sheen-Chen, S.M.1
  • 132
    • 34548085454 scopus 로고    scopus 로고
    • Focal Adhesion Kinase and p53 Signaling in Cancer Cells
    • DOI 10.1016/S0074-7696(07)63003-4, PII S0074769607630034, A Survey of Cell Biology
    • Golubovskaya V M and Cance W G 2007 Focal adhesion kinase and p53 signaling in cancer cells Int. Rev. Cytol. 263 103-53 (Pubitemid 47296394)
    • (2007) International Review of Cytology , vol.263 , pp. 103-153
    • Golubovskaya, V.M.1    Cance, W.G.2
  • 133
    • 80051980558 scopus 로고    scopus 로고
    • FAK regulates intestinal epithelial cell survival and proliferation during mucosal wound healing
    • 10.1371/journal.pone.0023123
    • Owen K A, Abshire M Y, Tilghman R W, Casanova J E and Bouton A H 2011 FAK regulates intestinal epithelial cell survival and proliferation during mucosal wound healing PLoS One 6 e23123
    • (2011) PLoS One , vol.6 , pp. 23123
    • Owen, K.A.1    Abshire, M.Y.2    Tilghman, R.W.3    Casanova, J.E.4    Bouton, A.H.5
  • 134
    • 84873313062 scopus 로고    scopus 로고
    • Function of focal adhesion kinase scaffolding to mediate endophilin A2 phosphorylation promotes epithelial-mesenchymal transition and mammary cancer stem cell activities in vivo
    • 10.1074/jbc.M112.420497
    • Fan H, Zhao X, Sun S, Luo M and Guan J L 2013 Function of focal adhesion kinase scaffolding to mediate endophilin A2 phosphorylation promotes epithelial-mesenchymal transition and mammary cancer stem cell activities in vivo J. Biol. Chem. 288 3322-33
    • (2013) J. Biol. Chem. , vol.288 , pp. 3322-3333
    • Fan, H.1    Zhao, X.2    Sun, S.3    Luo, M.4    Guan, J.L.5
  • 136
    • 84879414971 scopus 로고    scopus 로고
    • Integrin β5 contributes to the tumorigenic potential of breast cancer cells through the Src-FAK and MEK-ERK signaling pathways
    • 10.1038/onc.2012.320
    • Bianchi-Smiraglia A, Paesante S and Bakin A V 2012 Integrin β5 contributes to the tumorigenic potential of breast cancer cells through the Src-FAK and MEK-ERK signaling pathways Oncogene 32 3049-58
    • (2012) Oncogene , vol.32 , pp. 3049-3058
    • Bianchi-Smiraglia, A.1    Paesante, S.2    Bakin, A.V.3
  • 137
    • 84857406562 scopus 로고    scopus 로고
    • Focal adhesion kinase contributes to proliferative potential of ErbB2 mammary tumour cells but is dispensable for ErbB2 mammary tumour induction in vivo
    • 10.1186/bcr3131
    • Lahlou H, Sanguin-Gendreau V, Frame M C and Muller W J 2012 Focal adhesion kinase contributes to proliferative potential of ErbB2 mammary tumour cells but is dispensable for ErbB2 mammary tumour induction in vivo Breast Cancer Res. 14 R36
    • (2012) Breast Cancer Res. , vol.14 , pp. 36
    • Lahlou, H.1    Sanguin-Gendreau, V.2    Frame, M.C.3    Muller, W.J.4
  • 138
    • 0027967292 scopus 로고
    • A transmembrane-anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK
    • Chan P Y, Kanner S B, Whitney G and Aruffo A 1994 A transmembrane- anchored chimeric focal adhesion kinase is constitutively activated and phosphorylated at tyrosine residues identical to pp125FAK J. Biol. Chem. 269 20567-74
    • (1994) J. Biol. Chem. , vol.269 , pp. 20567-20574
    • Chan, P.Y.1    Kanner, S.B.2    Whitney, G.3    Aruffo, A.4
  • 139
    • 0242495710 scopus 로고    scopus 로고
    • Regulation of Focal Adhesion Kinase by Its Amino-Terminal Domain through an Autoinhibitory Interaction
    • DOI 10.1128/MCB.23.22.8030-8041.2003
    • Cooper L A, Shen T L and Guan J L 2003 Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction Mol. Cell Biol. 23 8030-41 (Pubitemid 37377496)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.22 , pp. 8030-8041
    • Cooper, L.A.1    Shen, T.-L.2    Guan, J.-L.3
  • 140
    • 0029834447 scopus 로고    scopus 로고
    • Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases
    • Schlaepfer D D and Hunter T 1996 Evidence for in vivo phosphorylation of the Grb2 SH2-domain binding site on focal adhesion kinase by Src-family protein-tyrosine kinases Mol. Cell Biol. 16 5623-33 (Pubitemid 26315082)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5623-5633
    • Schlaepfer, D.D.1    Hunter, T.2
  • 141
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the Focal Adhesion Kinase, pp125(FAK), to cellular focal adhesions
    • DOI 10.1083/jcb.123.4.993
    • Hildebrand J D, Schaller M D and Parsons J T 1993 Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK, to cellular focal adhesions J. Cell Biol. 123 993-1005 (Pubitemid 23333585)
    • (1993) Journal of Cell Biology , vol.123 , Issue.4 , pp. 993-1005
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 142
    • 84873827829 scopus 로고    scopus 로고
    • I3C and ICZ inhibit migration by suppressing the EMT process and FAK expression in breast cancer cells
    • Ho J N, Jun W, Choue R and Lee J 2013 I3C and ICZ inhibit migration by suppressing the EMT process and FAK expression in breast cancer cells Mol. Med. Rep. 7 384-8
    • (2013) Mol. Med. Rep. , vol.7 , pp. 384-388
    • Ho, J.N.1    Jun, W.2    Choue, R.3    Lee, J.4
  • 143
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • 10.1074/jbc.270.36.21206
    • Sasaki H, Nagura K, Ishino M, Tobioka H, Kotani K and Sasaki T 1995 Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily J. Biol. Chem. 270 21206-19
    • (1995) J. Biol. Chem. , vol.270 , pp. 21206-21219
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 144
    • 0028826350 scopus 로고
    • Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain
    • 10.1074/jbc.270.46.27742
    • Avraham S et al 1995 Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain J. Biol. Chem. 270 27742-51
    • (1995) J. Biol. Chem. , vol.270 , pp. 27742-27751
    • Avraham, S.1
  • 147
    • 0030944686 scopus 로고    scopus 로고
    • Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells
    • DOI 10.1074/jbc.272.22.14341
    • Li X and Earp H S 1997 Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells J. Biol. Chem. 272 14341-8 (Pubitemid 27232849)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.22 , pp. 14341-14348
    • Li, X.1    Earp, H.S.2
  • 148
    • 0030971847 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the novel protein-tyrosine kinase RAFTK during an early phase of platelet activation by an integrin glycoprotein IIb- IIIa-independent mechanism
    • DOI 10.1074/jbc.272.16.10941
    • Raja S, Avraham S and Avraham H 1997 Tyrosine phosphorylation of the novel protein-tyrosine kinase RAFTK during an early phase of platelet activation by an integrin glycoprotein IIb-IIIa-independent mechanism J. Biol. Chem. 272 10941-7 (Pubitemid 27181114)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.16 , pp. 10941-10947
    • Raja, S.1    Avraham, S.2    Avraham, H.3
  • 150
    • 0029978533 scopus 로고    scopus 로고
    • Characterization of RAFTK, a novel focal adhesion kinase, and its integrin-dependent phosphorylation and activation in megakaryocytes
    • Li J, Avraham H, Rogers R A, Raja S and Avraham S 1996 Characterization of RAFTK, a novel focal adhesion kinase, and its integrin-dependent phosphorylation and activation in megakaryocytes Blood 88 417-28 (Pubitemid 26240372)
    • (1996) Blood , vol.88 , Issue.2 , pp. 417-428
    • Li, J.1    Avraham, H.2    Rogers, R.A.3    Raja, S.4    Avraham, S.5
  • 151
    • 0031032421 scopus 로고    scopus 로고
    • 3 integrin which can induce the phosphorylation of focal adhesion kinase and the related PYK-2
    • DOI 10.1002/eji.1830270147
    • Ma E A, Lou O, Berg N N and Ostergaard H L 1997 Cytotoxic T lymphocytes express a β3 integrin which can induce the phosphorylation of focal adhesion kinase and the related Pyk-2 Eur. J. Immunol. 27 329-35 (Pubitemid 27046095)
    • (1997) European Journal of Immunology , vol.27 , Issue.1 , pp. 329-335
    • Ma, E.A.1    Lou, O.2    Berg, N.N.3    Ostergaard, H.L.4
  • 152
    • 0030771904 scopus 로고    scopus 로고
    • Differential signaling by the focal adhesion kinase and cell adhesion kinase β
    • DOI 10.1074/jbc.272.40.25319
    • Schaller M D and Sasaki T 1997 Differential signaling by the focal adhesion kinase and cell adhesion kinase beta J. Biol. Chem. 272 25319-25 (Pubitemid 27415723)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.40 , pp. 25319-25325
    • Schaller, M.D.1    Sasaki, T.2
  • 153
    • 0028289562 scopus 로고
    • Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: Identification of a vinculin and pp125FAK-binding region
    • Turner C E and Miller J T 1994 Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125FAK-binding region J. Cell Sci. 107 1583-91
    • (1994) J. Cell Sci. , vol.107 , pp. 1583-1591
    • Turner, C.E.1    Miller, J.T.2
  • 156
    • 0029891787 scopus 로고    scopus 로고
    • Human enhancer of filamentation 1, a novel p130CAS-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae
    • Law S F, Estojak J, Wang B, Mysliwiec T, Kruh G and Golemis E A 1996 Human enhancer of filamentation 1, a novel p130CAS-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae Mol. Cell Biol. 16 3327-37
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3327-3337
    • Law, S.F.1    Estojak, J.2    Wang, B.3    Mysliwiec, T.4    Kruh, G.5    Golemis, E.A.6
  • 157
    • 0031047981 scopus 로고    scopus 로고
    • Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs
    • DOI 10.1074/jbc.272.9.5501
    • Polte T R and Hanks S K 1997 Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(CAS)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs J. Biol. Chem. 272 5501-9 (Pubitemid 27102371)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.9 , pp. 5501-5509
    • Polte, T.R.1    Hanks, S.K.2
  • 158
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • DOI 10.1074/jbc.271.42.26329
    • Chen H C, Appeddu P A, Isoda H and Guan J L 1996 Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase J. Biol. Chem. 271 26329-34 (Pubitemid 26347485)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.42 , pp. 26329-26334
    • Chen, H.-C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.-L.4
  • 159
    • 0032525199 scopus 로고    scopus 로고
    • The related adhesion focal tyrosine kinase (RAFTK) is tyrosine phosphorylated and participates in colony-stimulating factor-1/macrophage colony-stimulating factor signaling in monocyte-macrophages
    • Hatch W C, Ganju R K, Hiregowdara D, Avraham S and Groopman J E 1998 The related adhesion focal tyrosine kinase (RAFTK) is tyrosine phosphorylated and participates in colony-stimulating factor-1/macrophage colony-stimulating factor signaling in monocyte-macrophages Blood 91 3967-73 (Pubitemid 28225767)
    • (1998) Blood , vol.91 , Issue.10 , pp. 3967-3973
    • Hatch, W.C.1    Ganju, R.K.2    Hiregowdara, D.3    Avraham, S.4    Groopman, J.E.5
  • 160
    • 0029770721 scopus 로고    scopus 로고
    • Activation of Pyk2 by stress signals and coupling with JNK signaling pathway
    • Tokiwa G, Dikic I, Lev S and Schlessinger J 1996 Activation of Pyk2 by stress signals and coupling with JNK signaling pathway Science 273 792-4 (Pubitemid 26271523)
    • (1996) Science , vol.273 , Issue.5276 , pp. 792-794
    • Tokiwa, G.1    Dikic, I.2    Lev, S.3    Schlessinger, J.4
  • 162
    • 0029907265 scopus 로고    scopus 로고
    • A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
    • DOI 10.1038/383547a0
    • Dikic I, Tokiwa G, Lev S, Courtneidge S A and Schlessinger J 1996 A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation Nature 383 547-50 (Pubitemid 26346184)
    • (1996) Nature , vol.383 , Issue.6600 , pp. 547-550
    • Dikic, I.1    Tokiwa, G.2    Lev, S.3    Courtneidge, S.A.4    Schlessinger, J.5
  • 163
    • 0030872062 scopus 로고    scopus 로고
    • Ras-dependent mitogen-activated protein kinase activation by G protein- coupled receptors
    • DOI 10.1074/jbc.272.31.19125
    • Della Rocca G J, van Biesen T, Daaka Y, Luttrell D K, Luttrell L M and Lefkowitz R J 1997 Ras-dependent mitogen-activated protein kinase activation by G protein-coupled receptors. Convergence of Gi- and Gq-mediated pathways on calcium/calmodulin, Pyk2, and Src kinase J. Biol. Chem. 272 19125-32 (Pubitemid 27337698)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.31 , pp. 19125-19132
    • Della Rocca, G.J.1    Van Biesen, T.2    Daaka, Y.3    Luttrell, D.K.4    Luttrell, L.M.5    Lefkowitz, R.J.6
  • 164
    • 0030926774 scopus 로고    scopus 로고
    • Focal adhesion kinase overexpression enhances Ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src
    • DOI 10.1074/jbc.272.20.13189
    • Schlaepfer D D and Hunter T 1997 Focal adhesion kinase overexpression enhances Ras-dependent integrin signaling to ERK2/mitogen-activated protein kinase through interactions with and activation of c-Src J. Biol. Chem. 272 13189-95 (Pubitemid 27216745)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.20 , pp. 13189-13195
    • Schlaepfer, D.D.1    Hunter, T.2
  • 165
    • 0031921101 scopus 로고    scopus 로고
    • Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: Summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events?
    • Schlaepfer D D, Jones K C and Hunter T 1998 Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events Mol. Cell Biol. 18 2571-85 (Pubitemid 28183427)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.5 , pp. 2571-2585
    • Schlaepfer, D.D.1    Jones, K.C.2    Hunter, T.3
  • 166
    • 0034731351 scopus 로고    scopus 로고
    • Focal adhesion kinase facilitates platelet-derived growth factor-BB-stimulated ERK2 activation required for chemotaxis migration of vascular smooth muscle cells
    • DOI 10.1074/jbc.M005450200
    • Hauck C R, Hsia D A and Schlaepfer D D 2000 Focal adhesion kinase facilitates platelet-derived growth factor-BB-stimulated ERK2 activation required for chemotaxis migration of vascular smooth muscle cells J. Biol. Chem. 275 41092-9 (Pubitemid 32054938)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.52 , pp. 41092-41099
    • Hauck, C.R.1    Hsia, D.A.2    Schlaepfer, D.D.3
  • 167
    • 0034725624 scopus 로고    scopus 로고
    • V-Src induces tyrosine phosphorylation of focal adhesion kinase independently of tyrosine 397 and formation of a complex with Src
    • DOI 10.1074/jbc.M909322199
    • McLean G W, Fincham V J and Frame M C 2000 v-Src induces tyrosine phosphorylation of focal adhesion kinase independently of tyrosine 397 and formation of a complex with Src J. Biol. Chem. 275 23333-9 (Pubitemid 30646235)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.30 , pp. 23333-23339
    • McLean, G.W.1    Fincham, V.J.2    Frame, M.C.3
  • 168
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase
    • 10.1038/372786a0 0028-0836
    • Schlaepfer D D, Hanks S K, Hunter T and van der Geer P 1994 Integrin-mediated signal transduction linked to Ras pathway by Grb2 binding to focal adhesion kinase Nature 372 786-91
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 169
    • 0033591228 scopus 로고    scopus 로고
    • Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades
    • DOI 10.1074/jbc.274.21.14893
    • Blaukat A, Ivankovic-Dikic I, Grönroos E, Dolfi F, Tokiwa G, Vuori K and Dikic I 1999 Adaptor proteins Grb2 and Crk couple Pyk2 with activation of specific mitogen-activated protein kinase cascades J. Biol. Chem. 274 14893-901 (Pubitemid 29265873)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.21 , pp. 14893-14901
    • Blaukat, A.1    Ivankovic-Dikic, I.2    Gronroos, E.3    Dolfi, F.4    Tokiwa, G.5    Vuori, K.6    Dikic, I.7
  • 170
    • 0030992148 scopus 로고    scopus 로고
    • RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes
    • DOI 10.1084/jem.185.6.1055
    • Ganju R K, Hatch W C, Avraham H, Ona M A, Druker B, Avraham S and Groopman J E 1997 RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes J. Exp. Med. 185 1055-63 (Pubitemid 27136798)
    • (1997) Journal of Experimental Medicine , vol.185 , Issue.6 , pp. 1055-1063
    • Ganju, R.K.1    Hatch, W.C.2    Avraham, H.3    Ona, M.A.4    Druker, B.5    Avraham, S.6    Groopman, J.E.7
  • 172
    • 17544364168 scopus 로고    scopus 로고
    • 2 but not for cytoskeletal organization
    • DOI 10.1074/jbc.271.25.14814
    • Clark E A and Hynes R O 1996 Ras activation is necessary for integrin-mediated activation of extracellular signal-regulated kinase 2 and cytosolic phospholipase A2 but not for cytoskeletal organization J. Biol. Chem. 271 14814-8 (Pubitemid 26194962)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.25 , pp. 14814-14818
    • Clark, E.A.1    Hynes, R.O.2
  • 173
    • 0030584077 scopus 로고    scopus 로고
    • The adaptor protein Shc couples a class of integrins to the control of cell cycle progression
    • DOI 10.1016/S0092-8674(00)81392-6
    • Wary K K, Mainiero F, Isakoff S J, Marcantonio E E and Giancotti F G 1996 The adaptor protein Shc couples a class of integrins to the control of cell cycle progression Cell 87 733-43 (Pubitemid 26386946)
    • (1996) Cell , vol.87 , Issue.4 , pp. 733-743
    • Wary, K.K.1    Mainiero, F.2    Isakoff, S.J.3    Marcantonio, E.E.4    Giancotti, F.G.5
  • 175
    • 0030293986 scopus 로고    scopus 로고
    • The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions
    • van der Geer P, Wiley S, Gish G D and Pawson T 1996 The Shc adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Y239/240) that mediate protein-protein interactions Curr. Biol. 6 1435-44 (Pubitemid 27012242)
    • (1996) Current Biology , vol.6 , Issue.11 , pp. 1435-1444
    • Van Der Geer, P.1    Wiley, S.2    Gish, G.D.3    Pawson, T.4
  • 176
    • 0028018234 scopus 로고
    • Potential role for focal adhesion kinase in migrating and proliferating keratinocytes near epidermal wounds and in culture
    • 1044-9523
    • Gates R E, King L E Jr, Hanks S K and Nanney L B 1984 Potential role for focal adhesion kinase in migrating and proliferating keratinocytes near epidermal wounds and in culture Cell Growth Differ. 5 891-9
    • (1984) Cell Growth Differ. , vol.5 , pp. 891-899
    • Gates, R.E.1    King, Jr.L.E.2    Hanks, S.K.3    Nanney, L.B.4
  • 177
    • 0029971297 scopus 로고    scopus 로고
    • A mechanism for regulation of the adhesion-associated protein tyrosine kinase pp125(FAK)
    • DOI 10.1038/380538a0
    • Richardson A and Parsons T 1996 A mechanism for regulation of the adhesion-associated proteintyrosine kinase pp125FAK Nature 380 538-40 (Pubitemid 26110644)
    • (1996) Nature , vol.380 , Issue.6574 , pp. 538-540
    • Richardson, A.1    Parsons, J.T.2
  • 178
    • 0030694182 scopus 로고    scopus 로고
    • Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: A role for paxillin tyrosine phosphorylation
    • Richardson A, Malik R K, Hildebrand J D and Parsons J T 1997 Inhibition of cell spreading by expression of the C-terminal domain of focal adhesion kinase (FAK) is rescued by coexpression of Src or catalytically inactive FAK: a role for paxillin tyrosine phosphorylation Mol. Cell Biol. 12 6906-14 (Pubitemid 27505920)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 6906-6914
    • Richardson, A.1    Malik, R.K.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 179
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation
    • Gilmore A P and Romer L H 1996 Inhibition of focal adhesion kinase (FAK) signaling in focal adhesions decreases cell motility and proliferation Mol. Biol. Cell 7 1209-24 (Pubitemid 26260738)
    • (1996) Molecular Biology of the Cell , vol.7 , Issue.8 , pp. 1209-1224
    • Gilmore, A.P.1    Romer, L.H.2
  • 180
    • 0032531732 scopus 로고    scopus 로고
    • - cell migration
    • DOI 10.1093/emboj/17.20.5933
    • Sieg D J, Ilić D, Jones K C, Damsky C H, Hunter T and Schlaepfer D D 1998 Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK-cell migration EMBO J. 17 5933-47 (Pubitemid 28474788)
    • (1998) EMBO Journal , vol.17 , Issue.20 , pp. 5933-5947
    • Sieg, D.J.1    Ilic, D.2    Jones, K.C.3    Damsky, C.H.4    Hunter, T.5    Schlaepfer, D.D.6
  • 184
    • 77954351473 scopus 로고    scopus 로고
    • Knock-in mutation reveals an essential role for focal adhesion kinase activity in blood vessel morphogenesis and cell motility-polarity but not cell proliferation
    • 10.1074/jbc.M110.129999
    • Lim S T, Chen X L, Tomar A, Miller N L, Yoo J and Schlaepfer D D 2010 Knock-in mutation reveals an essential role for focal adhesion kinase activity in blood vessel morphogenesis and cell motility-polarity but not cell proliferation J. Biol. Chem. 285 21526-36
    • (2010) J. Biol. Chem. , vol.285 , pp. 21526-21536
    • Lim, S.T.1    Chen, X.L.2    Tomar, A.3    Miller, N.L.4    Yoo, J.5    Schlaepfer, D.D.6
  • 185
    • 67650424259 scopus 로고    scopus 로고
    • The role of vinculin in the regulation of the mechanical properties of cells
    • 10.1007/s12013-009-9047-6 1085-9195
    • Mierke C T 2009 The role of vinculin in the regulation of the mechanical properties of cells Cell Biochem. Biophys. 53 115-26
    • (2009) Cell Biochem. Biophys. , vol.53 , pp. 115-126
    • Mierke, C.T.1
  • 187
    • 84873386319 scopus 로고    scopus 로고
    • The integrin αv β3 increases cellular stiffness and cytoskeletal remodeling dynamics to facilitate cancer cell invasion
    • 10.1088/1367-2630/15/1/015003 1367-2630 015003
    • Mierke C T 2013 The integrin αv β3 increases cellular stiffness and cytoskeletal remodeling dynamics to facilitate cancer cell invasion New J. Phys. 15 015003
    • (2013) New J. Phys. , vol.15 , Issue.1
    • Mierke, C.T.1
  • 190
    • 72049098196 scopus 로고    scopus 로고
    • Matrix densityinduced mechanoregulation of breast cell phenotype, signaling and gene expression through a FAK-ERK linkage
    • 10.1038/onc.2009.299
    • Provenzano P P, Inman D R, Eliceiri K W and Keely P J 2009 Matrix densityinduced mechanoregulation of breast cell phenotype, signaling and gene expression through a FAK-ERK linkage Oncogene 28 4326-43
    • (2009) Oncogene , vol.28 , pp. 4326-4343
    • Provenzano, P.P.1    Inman, D.R.2    Eliceiri, K.W.3    Keely, P.J.4
  • 191
    • 84880938029 scopus 로고    scopus 로고
    • Phagocytized beads reduce the invasiveness of highly-invasive cancer cells by regulating cellular stiffness
    • 10.1007/s12013-012-9506-3 1085-9195
    • Mierke C T 2013 Phagocytized beads reduce the invasiveness of highly-invasive cancer cells by regulating cellular stiffness Cell Biochem. Biophys. 66 599-622
    • (2013) Cell Biochem. Biophys. , vol.66 , pp. 599-622
    • Mierke, C.T.1
  • 193
    • 84875373346 scopus 로고    scopus 로고
    • Physical break-down of the classical view on cancer cell invasion and metastasis
    • 10.1016/j.ejcb.2012.12.002
    • Mierke C T 2013 Physical break-down of the classical view on cancer cell invasion and metastasis Eur. J. Cell Biol. 92 89-104
    • (2013) Eur. J. Cell Biol. , vol.92 , pp. 89-104
    • Mierke, C.T.1
  • 194
    • 80955166140 scopus 로고    scopus 로고
    • The biomechanical properties of 3d extracellular matrices and embedded cells regulate the invasiveness of cancer cells
    • 10.1007/s12013-011-9193-5 1085-9195
    • Mierke C T 2011 The biomechanical properties of 3d extracellular matrices and embedded cells regulate the invasiveness of cancer cells Cell Biochem. Biophys. 61 217-36
    • (2011) Cell Biochem. Biophys. , vol.61 , pp. 217-236
    • Mierke, C.T.1
  • 195
    • 34249864531 scopus 로고    scopus 로고
    • Biomechanics and biophysics of cancer cells
    • DOI 10.1016/j.actbio.2007.04.002, PII S174270610700061X
    • Suresh S 2007 Biomechanics and biophysics of cancer cells Acta Biomater. 3 413-38 (Pubitemid 46865787)
    • (2007) Acta Biomaterialia , vol.3 , Issue.4 , pp. 413-438
    • Suresh, S.1
  • 196
    • 80053422837 scopus 로고    scopus 로고
    • Contractile forces contribute to increased GPI-anchored receptor CD24 facilitated cancer cell invasion
    • 10.1074/jbc.M111.245183
    • Mierke C T, Bretz N and Altevogt P 2011 Contractile forces contribute to increased GPI-anchored receptor CD24 facilitated cancer cell invasion J. Biol. Chem. 286 34858-71
    • (2011) J. Biol. Chem. , vol.286 , pp. 34858-34871
    • Mierke, C.T.1    Bretz, N.2    Altevogt, P.3
  • 198
    • 84861110781 scopus 로고    scopus 로고
    • Endothelial cell's biomechanical properties are regulated by invasive cancer cells
    • 10.1039/c2mb25024a
    • Mierke C T 2012 Endothelial cell's biomechanical properties are regulated by invasive cancer cells Mol. Biosyst. 8 1639-49
    • (2012) Mol. Biosyst. , vol.8 , pp. 1639-1649
    • Mierke, C.T.1
  • 199
    • 77956472212 scopus 로고    scopus 로고
    • The role of the tissue microenvironment in the regulation of cancer cell motility and invasion
    • 10.1186/1478-811X-8-22
    • Brabek J, Mierke C T, Rösel D, Vesely P and Fabry B 2010 The role of the tissue microenvironment in the regulation of cancer cell motility and invasion Cell Commun. Signal 8 22
    • (2010) Cell Commun. Signal , vol.8 , pp. 22
    • Brabek, J.1    Mierke, C.T.2    Rösel, D.3    Vesely, P.4    Fabry, B.5
  • 200
    • 79551540808 scopus 로고    scopus 로고
    • Role of the endothelium during tumor cell metastasis: Is the endothelium a barrier or a promoter for cell invasion and metastasis?
    • 10.1155/2008/183516 0368-1432 183516
    • Mierke C T 2008 Role of the endothelium during tumor cell metastasis: Is the endothelium a barrier or a promoter for cell invasion and metastasis? J. Biophys. 2008 183516
    • (2008) J. Biophys. , vol.2008
    • Mierke, C.T.1
  • 201
    • 79951545991 scopus 로고    scopus 로고
    • Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1
    • 10.1021/ja109972p
    • Adhikari A S, Chai J and Dunn A R 2011 Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1 J. Am. Chem. Soc. 133 1686-9
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 1686-1689
    • Adhikari, A.S.1    Chai, J.2    Dunn, A.R.3
  • 204
    • 0031569914 scopus 로고    scopus 로고
    • New insights into integrin-ligand interaction
    • Loftus J C and Liddington R C 1997 Cell adhesion in vascular biology. New insights into integrin-ligand interaction J. Clin. Invest. 99 2302-6 (Pubitemid 27227703)
    • (1997) Journal of Clinical Investigation , vol.99 , Issue.10 , pp. 2302-2306
    • Loftus, J.C.1    Liddington, R.C.2
  • 206
    • 0021957079 scopus 로고
    • Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture
    • DOI 10.1083/jcb.100.5.1528
    • Damsky C H, Knudsen K A, Bradley D, Buck C A and Horwitz A F 1985 Distribution of the cell substratum attachment (CSAT) antigen on myogenic and fibroblastic cells in culture J. Cell Biol. 100 1528-39 (Pubitemid 15098029)
    • (1985) Journal of Cell Biology , vol.100 , Issue.5 , pp. 1528-1539
    • Damsky, C.H.1    Knudsen, K.A.2    Bradley, D.3
  • 207
    • 0023224549 scopus 로고
    • The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight β subunit
    • Hemler M E, Huang C and Schwarz L 1987 The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130 000 molecular weight beta subunit J. Biol. Chem. 262 3300-9 (Pubitemid 17127549)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.7 , pp. 3300-3309
    • Hemler, M.E.1    Huang, C.2    Schwarz, L.3
  • 208
    • 0020373648 scopus 로고
    • A monoclonal antibody detaches embryonic skeletal muscle from extracellular matrices
    • DOI 10.1083/jcb.95.2.654
    • Neff N T, Lowrey C, Decker C, Tovar A, Damsky C, Buck C and Horwitz A F 1982 A monoclonal antibody detaches embryonic skeletal muscle from extracellular matrices J. Cell Biol. 95 654-66 (Pubitemid 13215884)
    • (1982) Journal of Cell Biology , vol.95 , Issue.2 , pp. 654-666
    • Neff, N.T.1    Lowrey, C.2    Decker, C.3
  • 209
    • 79958111460 scopus 로고    scopus 로고
    • Loss of keratins 8 and 18 leads to alterations in α6β4- integrin-mediated signalling and decreased neoplastic progression in an oral-tumour-derived cell line
    • 10.1242/jcs.073585
    • Alam H, Kundu S T, Dalal S N and Vaidya M M 2011 Loss of keratins 8 and 18 leads to alterations in α6β4-integrin-mediated signalling and decreased neoplastic progression in an oral-tumour-derived cell line J. Cell Sci. 124 2096-106
    • (2011) J. Cell Sci. , vol.124 , pp. 2096-2106
    • Alam, H.1    Kundu, S.T.2    Dalal, S.N.3    Vaidya, M.M.4
  • 210
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Turner C E 2009 Paxillin interactions J. Cell Sci. 113 4139-40
    • (2009) J. Cell Sci. , vol.113 , pp. 4139-4140
    • Turner, C.E.1
  • 211
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • 10.1038/nrm2957
    • Parsons J T, Horwitz A R and Schwartz M A 2010 Cell adhesion: integrating cytoskeletal dynamics and cellular tension Nat. Rev. Mol. Cell Biol. 11 633-43
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 212
    • 80053925801 scopus 로고    scopus 로고
    • Cell-matrix adhesions in 3D
    • 10.1016/j.matbio.2011.06.001
    • Harunaga J S and Yamada K M 2011 Cell-matrix adhesions in 3D Matrix Biol. 30 363-8
    • (2011) Matrix Biol. , vol.30 , pp. 363-368
    • Harunaga, J.S.1    Yamada, K.M.2
  • 213
    • 78650457713 scopus 로고    scopus 로고
    • Reducing background fluorescence reveals adhesions in 3D matrices
    • 10.1038/ncb0111-3 1465-7392
    • Kubow K E and Horwitz A R 2011 Reducing background fluorescence reveals adhesions in 3D matrices Nat. Cell Biol. 13 3-5
    • (2011) Nat. Cell Biol. , vol.13 , pp. 3-5
    • Kubow, K.E.1    Horwitz, A.R.2
  • 215
    • 77952350971 scopus 로고    scopus 로고
    • Keratin 8/18 modulation of protein kinase C-mediated integrin-dependent adhesion and migration of liver epithelial cells
    • 10.1091/mbc.E09-05-0373 1059-1524
    • Bordeleau F, Galarneau L, Gilbert S, Loranger A and Marceau N 2010 Keratin 8/18 modulation of protein kinase C-mediated integrin-dependent adhesion and migration of liver epithelial cells Mol. Biol. Cell 21 1698-713
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1698-1713
    • Bordeleau, F.1    Galarneau, L.2    Gilbert, S.3    Loranger, A.4    Marceau, N.5
  • 216
    • 69449103232 scopus 로고    scopus 로고
    • A FAK-p120RasGAP-p190RhoGAP complex regulates polarity in migrating cells
    • 10.1242/jcs.046870
    • Tomar A, Lim S T, Lim Y and Schlaepfer D D 2009 A FAK-p120RasGAP- p190RhoGAP complex regulates polarity in migrating cells J. Cell Sci. 122 1852-62
    • (2009) J. Cell Sci. , vol.122 , pp. 1852-1862
    • Tomar, A.1    Lim, S.T.2    Lim, Y.3    Schlaepfer, D.D.4
  • 218
    • 57349157913 scopus 로고    scopus 로고
    • Mechanosensing machinery for cells under low substratum rigidity
    • 10.1152/ajpcell.00223.2008 0363-6143
    • Wei W C, Lin H H, Shen M R and Tang M J 2008 Mechanosensing machinery for cells under low substratum rigidity Am. J. Physiol. Cell Physiol. 295 C1579-89
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295
    • Wei, W.C.1    Lin, H.H.2    Shen, M.R.3    Tang, M.J.4
  • 222
    • 58149288236 scopus 로고    scopus 로고
    • The differential amino acid requirement within osteopontin in α4 and α9 integrin-mediated cell binding and migration
    • 10.1016/j.matbio.2008.10.002
    • Ito K et al 2009 The differential amino acid requirement within osteopontin in α4 and α9 integrin-mediated cell binding and migration Matrix Biol. 28 11-9
    • (2009) Matrix Biol. , vol.28 , pp. 11-19
    • Ito, K.1
  • 223
    • 0033527623 scopus 로고    scopus 로고
    • Cell migration - Movin' on
    • DOI 10.1126/science.286.5442.1102
    • Horwitz A R and Parsons J T 1999 Cell migration - movin' on Science 286 1102-3 (Pubitemid 29522263)
    • (1999) Science , vol.286 , Issue.5442 , pp. 1102-1103
    • Horwitz, A.R.1    Parsons, J.T.2
  • 225
    • 33947261720 scopus 로고    scopus 로고
    • Integrin α6 cleavage: A novel modification to modulate cell migration
    • DOI 10.1016/j.yexcr.2007.01.006, PII S0014482707000195
    • Pawar S C, Demetriou M C, Nagle R B, Bowden G T and Cress A E 2007 Integrin α6 cleavage: a novel modification to modulate cell migration Exp. Cell Res. 313 1080-9 (Pubitemid 46427820)
    • (2007) Experimental Cell Research , vol.313 , Issue.6 , pp. 1080-1089
    • Pawar, S.C.1    Demetriou, M.C.2    Nagle, R.B.3    Bowden, G.T.4    Cress, A.E.5
  • 226
    • 1642367158 scopus 로고    scopus 로고
    • α5β1, αVβ3 and the platelet-associated integrin αIIbβ3 coordinately regulate adhesion and migration of differentiating mouse trophoblast cells
    • DOI 10.1016/j.ydbio.2003.12.010, PII S0012160603007917
    • Rout U K, Wang J, Paria B C and Armant D R 2004 α5β1, αVβ3 and the platelet-associated integrin αIIbβ3 coordinately regulate adhesion and migration of differentiating mouse trophoblast cells Dev. Biol. 268 135-51 (Pubitemid 38367856)
    • (2004) Developmental Biology , vol.268 , Issue.1 , pp. 135-151
    • Rout, U.K.1    Wang, J.2    Paria, B.C.3    Armant, D.R.4
  • 227
    • 0037821712 scopus 로고    scopus 로고
    • 3-mediated adhesion and migration on fibrinogen
    • DOI 10.1074/jbc.M212538200
    • Ly D P, Zazzali K M and Corbett S A 2003 De novo expression of the integrin α5β1 regulates αvβ3-mediated adhesion and migration on fibrinogen J. Biol. Chem. 278 21878-85 (Pubitemid 36792594)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21878-21885
    • Ly, D.P.1    Zazzali, K.M.2    Corbett, S.A.3
  • 228
    • 69249129752 scopus 로고    scopus 로고
    • Up-regulation of α5-integrin by E-cadherin loss in hypoxia and its key role in the migration of extravillous trophoblast cells during early implantation
    • 10.1210/en.2008-1662
    • Arimoto-Ishida E et al 2009 Up-regulation of α5-integrin by E-cadherin loss in hypoxia and its key role in the migration of extravillous trophoblast cells during early implantation Endocrinology 150 4306-15
    • (2009) Endocrinology , vol.150 , pp. 4306-4315
    • Arimoto-Ishida, E.1
  • 230
    • 33749461921 scopus 로고    scopus 로고
    • Positive expression of E-cadherin suppresses cell adhesion to fibronectin via reduction of α5β1 integrin in human breast carcinoma cells
    • DOI 10.1007/s00432-006-0128-2
    • Wu H, Liang Y L, Li Z, Jin J, Zhang W, Duan L and Zha X 2006 Positive expression of E-cadherin suppresses cell adhesion to fibronectin via reduction of α5β1 integrin in human breast carcinoma cells J. Cancer Res. Clin. Oncol. 132 795-803 (Pubitemid 44521455)
    • (2006) Journal of Cancer Research and Clinical Oncology , vol.132 , Issue.12 , pp. 795-803
    • Wu, H.1    Liang, Y.-L.2    Li, Z.3    Jin, J.4    Zhang, W.5    Duan, L.6    Zha, X.7
  • 233
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary L A, Chang J F and Guan J L 1996 Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn J. Cell Sci. 109 1787-94 (Pubitemid 26248624)
    • (1996) Journal of Cell Science , vol.109 , Issue.7 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.-L.3
  • 234
    • 33746031475 scopus 로고    scopus 로고
    • An inhibitory role for FAK in regulating proliferation: A link between limited adhesion and RhoA-ROCK signaling
    • DOI 10.1083/jcb.200510062
    • Pirone D M, Liu W F, Ruiz S A, Gao L, Raghavan S, Lemmon C A, Romer L H and Chen C S 2006 An inhibitory role for FAK in regulating proliferation: a link between limited adhesion and RhoA-ROCK signaling J. Cell Biol. 174 277-88 (Pubitemid 44079862)
    • (2006) Journal of Cell Biology , vol.174 , Issue.2 , pp. 277-288
    • Pirone, D.M.1    Liu, W.F.2    Ruiz, S.A.3    Gao, L.4    Raghavan, S.5    Lemmon, C.A.6    Romer, L.H.7    Chen, C.S.8
  • 235
    • 0344306445 scopus 로고    scopus 로고
    • Repositioning of cells by mechanotaxis on surfaces with micropatterned Young's modulus
    • Gray D S, Tien J and Chen C S 2003 Repositioning of cells by mechanotaxis on surfaces with micropatterned Young's modulus J. Biomed. Mater. Res. A 66 605-14 (Pubitemid 37517206)
    • (2003) Journal of Biomedical Materials Research - Part A , vol.66 , Issue.3 , pp. 605-614
    • Gray, D.S.1    Tien, J.2    Chen, C.S.3
  • 236
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo C M, Wang H B, Dembo M and Wang Y L 2000 Cell movement is guided by the rigidity of the substrate Biophys. J. 79 144-52 (Pubitemid 30436733)
    • (2000) Biophysical Journal , vol.79 , Issue.1 , pp. 144-152
    • Lo, C.-M.1    Wang, H.-B.2    Dembo, M.3    Wang, Y.-L.4
  • 237
    • 84855716430 scopus 로고    scopus 로고
    • Multi-gradient hydrogels produced layer by layer with capillary flow and crosslinking in open microchannels
    • 10.1039/c2lc20515g
    • Piraino F, Camci-Unal G, Hancock M J, Rasponi M and Khademhosseini A 2012 Multi-gradient hydrogels produced layer by layer with capillary flow and crosslinking in open microchannels Lab. Chip 12 659-61
    • (2012) Lab. Chip , vol.12 , pp. 659-661
    • Piraino, F.1    Camci-Unal, G.2    Hancock, M.J.3    Rasponi, M.4    Khademhosseini, A.5
  • 238
    • 76249088362 scopus 로고    scopus 로고
    • Matrix architecture dictates three-dimensional migration modes of human macrophages: Differential involvement of proteases and podosome-like structures
    • 10.4049/jimmunol.0902223
    • Van Goethem E, Poincloux R, Gauffre F, Maridonneau-Parini I and Le Cabec V 2010 Matrix architecture dictates three-dimensional migration modes of human macrophages: differential involvement of proteases and podosome-like structures J. Immunol. 184 1049-61
    • (2010) J. Immunol. , vol.184 , pp. 1049-1061
    • Van Goethem, E.1    Poincloux, R.2    Gauffre, F.3    Maridonneau-Parini, I.4    Le Cabec, V.5
  • 239
    • 79952129858 scopus 로고    scopus 로고
    • Direct comparisons of the morphology, migration, cell adhesions, and actin cytoskeleton of fibroblasts in four different three-dimensional extracellular matrices
    • 10.1089/ten.tea.2010.0273 1076-3279 A
    • Hakkinen K M, Harunaga J S, Doyle A D and Yamada K M 2011 Direct comparisons of the morphology, migration, cell adhesions, and actin cytoskeleton of fibroblasts in four different three-dimensional extracellular matrices Tissue Eng. A 17 713-24
    • (2011) Tissue Eng. , vol.17 , pp. 713-724
    • Hakkinen, K.M.1    Harunaga, J.S.2    Doyle, A.D.3    Yamada, K.M.4
  • 240
    • 84862823381 scopus 로고    scopus 로고
    • Biophysical control of invasive tumor cell behavior by extracellular matrix microarchitecture
    • 10.1016/j.biomaterials.2012.02.029 0142-9612
    • Carey S P, Kraning-Rush C M, Williams R M and Reinhart-King C A 2012 Biophysical control of invasive tumor cell behavior by extracellular matrix microarchitecture Biomaterials 33 4157-65
    • (2012) Biomaterials , vol.33 , pp. 4157-4165
    • Carey, S.P.1    Kraning-Rush, C.M.2    Williams, R.M.3    Reinhart-King, C.A.4
  • 241
    • 77953959860 scopus 로고    scopus 로고
    • The differential regulation of cell motile activity through matrix stiffness and porosity in three dimensional collagen matrices
    • 10.1016/j.biomaterials.2010.04.064 0142-9612
    • Miron-Mendoza M, Seemann J and Grinnell F 2010 The differential regulation of cell motile activity through matrix stiffness and porosity in three dimensional collagen matrices Biomaterials 31 6425-35
    • (2010) Biomaterials , vol.31 , pp. 6425-6435
    • Miron-Mendoza, M.1    Seemann, J.2    Grinnell, F.3
  • 242
    • 0028068868 scopus 로고
    • Biased cell migration of fibroblasts exhibiting contact guidance in oriented collagen gels
    • DOI 10.1007/BF02368241
    • Dickinson R B, Guido S and Tranquillo R T 1994 Biased cell migration of fibroblasts exhibiting contact guidance in oriented collagen gels Ann. Biomed. Eng. 22 342-56 (Pubitemid 24264082)
    • (1994) Annals of Biomedical Engineering , vol.22 , Issue.4 , pp. 342-356
    • Dickinson, R.B.1    Guido, S.2    Tranquillo, R.T.3
  • 243
    • 80155133565 scopus 로고    scopus 로고
    • Engineering 3D cell instructive microenvironments by rational assembly of artificial extracellular matrices and cell patterning
    • 10.1039/c1ib00045d
    • Sala A, Hänseler P, Ranga A, Lutolf M P, Vörös J, Ehrbar M and Weber F E 2011 Engineering 3D cell instructive microenvironments by rational assembly of artificial extracellular matrices and cell patterning Integr. Biol. (Camb.) 3 1102-11
    • (2011) Integr. Biol. (Camb.) , vol.3 , pp. 1102-1111
    • Sala, A.1    Hänseler, P.2    Ranga, A.3    Lutolf, M.P.4    Vörös, J.5    Ehrbar, M.6    Weber, F.E.7
  • 244
    • 81155160131 scopus 로고    scopus 로고
    • Engineering extracellular matrix structure in 3D multiphase tissues
    • 10.1016/j.biomaterials.2011.05.043 0142-9612
    • Gillette B M, Rossen N S, Das N, Leong D, Wang M, Dugar A and Sia S K 2011 Engineering extracellular matrix structure in 3D multiphase tissues Biomaterials 32 8067-76
    • (2011) Biomaterials , vol.32 , pp. 8067-8076
    • Gillette, B.M.1    Rossen, N.S.2    Das, N.3    Leong, D.4    Wang, M.5    Dugar, A.6    Sia, S.K.7
  • 245
    • 33845765615 scopus 로고    scopus 로고
    • A collagen-based interface construct for the assessment of cell-dependent mechanical integration of tissue surfaces
    • DOI 10.1007/s00441-006-0316-z
    • Marenzana M, Kelly D J, Prendergast P J and Brown R A 2007 A collagen-based interface construct for the assessment of cell-dependent mechanical integration of tissue surfaces Cell Tissue Res. 327 293-300 (Pubitemid 46011240)
    • (2007) Cell and Tissue Research , vol.327 , Issue.2 , pp. 293-300
    • Marenzana, M.1    Kelly, D.J.2    Prendergast, P.J.3    Brown, R.A.4
  • 246
    • 84861670229 scopus 로고    scopus 로고
    • Individual versus collective fibroblast spreading and migration: Regulation by matrix composition in 3D culture
    • 10.1016/j.exer.2012.03.015
    • Miron-Mendoza M, Lin X, Ma L, Ririe P and Petroll W M 2012 Individual versus collective fibroblast spreading and migration: regulation by matrix composition in 3D culture Exp. Eye Res. 99 36-44
    • (2012) Exp. Eye Res. , vol.99 , pp. 36-44
    • Miron-Mendoza, M.1    Lin, X.2    Ma, L.3    Ririe, P.4    Petroll, W.M.5
  • 247
    • 0031745571 scopus 로고    scopus 로고
    • Signal transduction and signal modulation by cell adhesion receptors: The role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins
    • Aplin A E, Howe A, Alahari S K and Juliano R L 1998 Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins Pharmacol. Rev. 50 197-263 (Pubitemid 28304026)
    • (1998) Pharmacological Reviews , vol.50 , Issue.2 , pp. 197-263
    • Aplin, A.E.1    Howe, A.2    Alahari, S.K.3    Juliano, R.L.4
  • 248
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • DOI 10.1093/emboj/16.10.2783
    • Khwaja A, Rodriguez-Viciana P, Wennström S, Warne P H and Downward J 1997 Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway EMBO J. 16 2783-93 (Pubitemid 27226215)
    • (1997) EMBO Journal , vol.16 , Issue.10 , pp. 2783-2793
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 250
    • 0032562682 scopus 로고    scopus 로고
    • The activation of p38 and apoptosis by the inhibition of Erk is antagonized by the phosphoinositide 3-kinase/Akt pathway
    • DOI 10.1074/jbc.273.17.10792
    • Berra E, Diaz-Meco M T and Moscat J 1998 The activation of p38 and apoptosis by the inhibition of ERK is antagonized by the phosphoinositide 3-kinase/Akt pathway J. Biol. Chem. 273 10792-7 (Pubitemid 28227697)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.17 , pp. 10792-10797
    • Berra, E.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 252
    • 0034599542 scopus 로고    scopus 로고
    • Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix
    • DOI 10.1083/jcb.149.1.223
    • Cho S Y and Klemke R L 2000 Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix J. Cell Biol. 149 223-36 (Pubitemid 30196711)
    • (2000) Journal of Cell Biology , vol.149 , Issue.1 , pp. 223-236
    • Cho, S.Y.1    Klemke, R.L.2
  • 253
    • 84863148727 scopus 로고    scopus 로고
    • RhoA/ROCK, cytoskeletal dynamics, and focal adhesion kinase are required for mechanical stretch-induced tenogenic differentiation of human mesenchymal stem cells
    • 10.1002/jcp.23016
    • Xu B, Song G, Ju Y, Li X, Song Y and Watanabe S 2012 RhoA/ROCK, cytoskeletal dynamics, and focal adhesion kinase are required for mechanical stretch-induced tenogenic differentiation of human mesenchymal stem cells J. Cell Physiol. 227 2722-9
    • (2012) J. Cell Physiol. , vol.227 , pp. 2722-2729
    • Xu, B.1    Song, G.2    Ju, Y.3    Li, X.4    Song, Y.5    Watanabe, S.6
  • 254
    • 75949111478 scopus 로고    scopus 로고
    • Activation of RhoA and FAK induces ERK-mediated osteopontin expression in mechanical force-subjected periodontal ligament fibroblasts
    • 10.1007/s11010-009-0276-1 0300-8177
    • Hong S Y, Jeon Y M, Lee H J, Kim J G, Baek J A and Lee J C 2010 Activation of RhoA and FAK induces ERK-mediated osteopontin expression in mechanical force-subjected periodontal ligament fibroblasts Mol. Cell Biochem. 335 263-72
    • (2010) Mol. Cell Biochem. , vol.335 , pp. 263-272
    • Hong, S.Y.1    Jeon, Y.M.2    Lee, H.J.3    Kim, J.G.4    Baek, J.A.5    Lee, J.C.6
  • 255
    • 84875228023 scopus 로고    scopus 로고
    • Osteopontin promotes mesenchymal stem cell migration and lessens cell stiffness via integrin β1, FAK, and ERK pathways
    • 10.1007/s12013-012-9449-8 1085-9195
    • Zou C, Luo Q, Qin J, Shi Y, Yang L, Ju B and Song G 2013 Osteopontin promotes mesenchymal stem cell migration and lessens cell stiffness via integrin β1, FAK, and ERK pathways Cell Biochem. Biophys. 65 455-62
    • (2013) Cell Biochem. Biophys. , vol.65 , pp. 455-462
    • Zou, C.1    Luo, Q.2    Qin, J.3    Shi, Y.4    Yang, L.5    Ju, B.6    Song, G.7
  • 256
    • 37249047361 scopus 로고    scopus 로고
    • Focal adhesion kinase as a regulator of cell tension in the progression of cancer
    • DOI 10.1016/j.semcancer.2007.08.002, PII S1044579X07000727
    • Tilghman R W and Parsons J T 2008 Focal adhesion kinase as a regulator of cell tension in the progression of cancer Semin. Cancer Biol. 18 45-52 (Pubitemid 350266368)
    • (2008) Seminars in Cancer Biology , vol.18 , Issue.1 , pp. 45-52
    • Tilghman, R.W.1    Parsons, J.T.2
  • 257
    • 84876329949 scopus 로고    scopus 로고
    • Akt1 promotes focal adhesion disassembly and cell motility through phosphorylation of FAK in growth factor-stimulated cells
    • 10.1242/jcs.112722
    • Higuchi M, Kihara R, Okazaki T, Aoki I, Suetsugu S and Gotoh Y 2012 Akt1 promotes focal adhesion disassembly and cell motility through phosphorylation of FAK in growth factor-stimulated cells J. Cell Sci. 126 745-55
    • (2012) J. Cell Sci. , vol.126 , pp. 745-755
    • Higuchi, M.1    Kihara, R.2    Okazaki, T.3    Aoki, I.4    Suetsugu, S.5    Gotoh, Y.6
  • 259
    • 0036293439 scopus 로고    scopus 로고
    • Intact vinculin protein is required for control of cell shape, cell mechanics, and rac-dependent lamellipodia formation
    • DOI 10.1006/bbrc.2001.6243
    • Goldmann W H and Ingber D E 2002 Intact vinculin protein is required for control of cell shape, cell mechanics, and rac-dependent lamellipodia formation Biochem. Biophys. Res. Commun. 290 749-55 (Pubitemid 34687504)
    • (2002) Biochemical and Biophysical Research Communications , vol.290 , Issue.2 , pp. 749-755
    • Goldmann, W.H.1    Ingber, D.E.2
  • 260
    • 0032516467 scopus 로고    scopus 로고
    • A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers
    • DOI 10.1021/bi9727242
    • Johnson R P, Niggli V, Durrer P and Craig S W 1998 A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers Biochemistry 37 10211-22 (Pubitemid 28366377)
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 10211-10222
    • Johnson, R.P.1    Niggli, V.2    Durrer, P.3    Craig, S.W.4
  • 261
    • 79955017821 scopus 로고    scopus 로고
    • Endothelial activation, dysfunction and permeability during severe infections
    • 10.1097/MOH.0b013e328345a3d1
    • Lee W L and Liles W C 2011 Endothelial activation, dysfunction and permeability during severe infections Curr. Opin. Hematol. 18 191-6
    • (2011) Curr. Opin. Hematol. , vol.18 , pp. 191-196
    • Lee, W.L.1    Liles, W.C.2
  • 262
    • 82955188761 scopus 로고    scopus 로고
    • Neutrophil transmigration, focal adhesion kinase and endothelial barrier function
    • 10.1016/j.mvr.2011.06.015
    • Yuan S Y, Shen Q, Rigor R R and Wu M H 2012 Neutrophil transmigration, focal adhesion kinase and endothelial barrier function Microvasc. Res. 83 82-8
    • (2012) Microvasc. Res. , vol.83 , pp. 82-88
    • Yuan, S.Y.1    Shen, Q.2    Rigor, R.R.3    Wu, M.H.4
  • 264
    • 0035184161 scopus 로고    scopus 로고
    • Reduced expression of junctional adhesion molecule and platelet/endothelial cell adhesion molecule-1 (CD31) at human vascular endothelial junctions by cytokines tumor necrosis factor-α plus interferon-γ does not reduce leukocyte transmigration under flow
    • Shaw S K, Perkins B N, Lim Y C, Liu Y, Nusrat A, Schnell F J, Parkos C A and Luscinskas F W 2001 Reduced expression of junctional adhesion molecule and platelet/endothelial cell adhesion molecule-1 (CD31) at human vascular endothelial junctions by cytokines tumor necrosis factor-alpha plus interferon-gamma does not reduce leukocyte transmigration under flow Am. J. Pathol. 159 2281-91 (Pubitemid 33104281)
    • (2001) American Journal of Pathology , vol.159 , Issue.6 , pp. 2281-2291
    • Shaw, S.K.1    Perkins, B.N.2    Lim, Y.-C.3    Liu, Y.4    Nusrat, A.5    Schnell, F.J.6    Parkos, C.A.7    Luscinskas, F.W.8
  • 265
    • 67650413623 scopus 로고    scopus 로고
    • Endothelial cell activation leads to neutrophil transmigration as supported by the sequential roles of ICAM-2, JAM-A, and PECAM-1
    • 10.1182/blood-2008-11-188375
    • Woodfin A, Voisin M B, Imhof B A, Dejana E, Engelhardt B and Nourshargh S 2009 Endothelial cell activation leads to neutrophil transmigration as supported by the sequential roles of ICAM-2, JAM-A, and PECAM-1 Blood 113 6246-57
    • (2009) Blood , vol.113 , pp. 6246-6257
    • Woodfin, A.1    Voisin, M.B.2    Imhof, B.A.3    Dejana, E.4    Engelhardt, B.5    Nourshargh, S.6
  • 267
    • 0347991870 scopus 로고    scopus 로고
    • Pressure Activates Colon Cancer Cell Adhesion by Inside-Out Focal Adhesion Complex and Actin Cytoskeletal Signaling
    • DOI 10.1053/j.gastro.2003.10.078
    • Thamilselvan V and Basson M D 2004 Pressure activates colon cancer cell adhesion by inside-out focal adhesion complex and actin cytoskeletal signaling Gastroenterology 126 8-18 (Pubitemid 38040719)
    • (2004) Gastroenterology , vol.126 , Issue.1 SUPPL. 1 , pp. 8-18
    • Thamilselvan, V.1    Basson, M.D.2
  • 268
    • 8544259557 scopus 로고    scopus 로고
    • Extracellular pressure stimulates colon cancer cell adhesion in vitro and to surgical wounds by Src (sarcoma protein) activation
    • DOI 10.1016/j.amjsurg.2004.07.005, PII S0002961004003356
    • Van der Voort van Zyp J, Thamilselvan V, Walsh M, Polin L and Basson M D 2004 Extracellular pressure stimulates colon cancer cell adhesion in vitro and to surgical wounds by Src (sarcoma protein) activation Am. J. Surg. 188 467-73 (Pubitemid 39491087)
    • (2004) American Journal of Surgery , vol.188 , Issue.5 , pp. 467-473
    • Van Der Voort Van Zyp, J.1    Thamilselvan, V.2    Walsh, M.3    Polin, L.4    Basson, M.D.5
  • 270
    • 27144544079 scopus 로고    scopus 로고
    • The role of the cytoskeleton in differentially regulating pressure-mediated effects on malignant colonocyte focal adhesion signaling and cell adhesion
    • DOI 10.1093/carcin/bgi135
    • Thamilselvan V and Basson M D 2005 The role of the cytoskeleton in differentially regulating pressure-mediated effects on malignant colonocyte focal adhesion signaling and cell adhesion Carcinogenesis 26 1687-97 (Pubitemid 41487984)
    • (2005) Carcinogenesis , vol.26 , Issue.10 , pp. 1687-1697
    • Thamilselvan, V.1    Basson, M.D.2
  • 271
    • 0036091414 scopus 로고    scopus 로고
    • The role of αvβ3 in prostate cancer progression
    • 10.1038/sj.neo.7900224
    • Cooper C R, Chay C H and Pienta K J 2002 The role of αvβ3 in prostate cancer progression Neoplasia 4 191-4
    • (2002) Neoplasia , vol.4 , pp. 191-194
    • Cooper, C.R.1    Chay, C.H.2    Pienta, K.J.3
  • 272
    • 0034934354 scopus 로고    scopus 로고
    • Hepatocyte growth factor induces colonic cancer cell invasiveness via enhanced motility and protease overproduction. Evidence for P13 kinase and PKC involvement
    • Kermorgant S, Aparicio T, Dessirier V, Lewin M J and Lehy T 2001 Hepatocyte growth factor induces colonic cancer cell invasiveness via enhanced motility and protease overproduction. Evidence for PI3 kinase and PKC involvement Carcinogenesis 22 1035-42 (Pubitemid 32633601)
    • (2001) Carcinogenesis , vol.22 , Issue.7 , pp. 1035-1042
    • Kermorgant, S.1    Aparicio, T.2    Dessirier, V.3    Lewin, M.J.M.4    Lehy, T.5
  • 273
    • 20444380697 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase accelerates postoperative tumor growth by inhibiting apoptosis and enhancing resistance to chemotherapy-induced apoptosis: Novel role for an old enemy
    • DOI 10.1074/jbc.M414696200
    • Coffey J C, Wang J H, Smith M J, Laing A, Bouchier-Hayes D, Cotter T G and Redmond H P 2005 Phosphoinositide 3-kinase accelerates postoperative tumor growth by inhibiting apoptosis and enhancing resistance to chemotherapy-induced apoptosis. Novel role for an old enemy J. Biol. Chem. 280 20968-77 (Pubitemid 40805654)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 20968-20977
    • Coffey, J.C.1    Wang, J.H.2    Smith, M.J.F.3    Laing, A.4    Bouchier-Hayes, D.5    Cotter, T.G.6    Redmond, H.P.7
  • 275
    • 0032125580 scopus 로고    scopus 로고
    • Increased levels of phosphatidylinositol 3-kinase activity in colorectal tumors
    • DOI 10.1002/(SICI)1097-0142(19980701)83:1<41::AID-CNCR6>3.0.CO;2-H
    • Phillips W A, St Clair F, Munday A D, Thomas R J and Mitchell C A 1998 Increased levels of phosphatidylinositol 3-kinase activity in colorectal tumors Cancer 83 41-7 (Pubitemid 28299627)
    • (1998) Cancer , vol.83 , Issue.1 , pp. 41-47
    • Phillips, W.A.1    St. Clair, F.2    Munday, A.D.3    Thomas, R.J.S.4    Mitchell, C.A.5
  • 278
    • 0037333465 scopus 로고    scopus 로고
    • 12 receptor blockade inhibits shear-induced platelet phosphatidylinositol 3-kinase activation
    • DOI 10.1124/mol.63.3.639
    • Resendiz J C, Feng S, Ji G, Francis K A, Berndt M C and Kroll M H 2003 Purinergic P2Y12 receptor blockade inhibits shear-induced platelet phosphatidylinositol 3-kinase activation Mol. Pharmacol. 63 639-45 (Pubitemid 36297335)
    • (2003) Molecular Pharmacology , vol.63 , Issue.3 , pp. 639-645
    • Resendiz, J.C.1    Feng, S.2    Ji, G.3    Francis, K.A.4    Berndt, M.C.5    Kroll, M.H.6
  • 279
    • 0027198412 scopus 로고
    • A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3- kinase binds the 110-kDa catalytic subunit in vivo
    • Klippel A, Escobedo J A, Hu Q and Williams L T 1993 A region of the 85-kilodalton (kDa) subunit of phosphatidylinositol 3-kinase binds the 110-kDa catalytic subunit in vivo Mol. Cell Biol. 13 5560-6 (Pubitemid 23260658)
    • (1993) Molecular and Cellular Biology , vol.13 , Issue.9 , pp. 5560-5566
    • Klippel, A.1    Escobedo, J.A.2    Hu, Q.3    Williams, L.T.4
  • 280
    • 0037096804 scopus 로고    scopus 로고
    • Phosphorylation of Akt/PKB is required for suppression of cancer cell apoptosis and tumor progression in human colorectal carcinoma
    • DOI 10.1002/cncr.10591
    • Itoh N, Semba S, Ito M, Takeda H, Kawata S and Yamakawa M 2002 Phosphorylation of Akt/PKB is required for suppression of cancer cell apoptosis and tumor progression in human colorectal carcinoma Cancer 94 3127-34 (Pubitemid 34670495)
    • (2002) Cancer , vol.94 , Issue.12 , pp. 3127-3134
    • Itoh, N.1    Semba, S.2    Ito, M.3    Takeda, H.4    Kawata, S.5    Yamakawa, M.6
  • 281
    • 1642578897 scopus 로고    scopus 로고
    • The phosphatidylinositol-3 kinase pathway regulates bladder cancer cell invasion
    • DOI 10.1111/j.1464-410X.2004.04574.x
    • Wu X, Obata T, Khan Q, Highshaw R A, De Vere White R and Sweeney C 2004 The phosphatidylinositol-3 kinase pathway regulates bladder cancer cell invasion BJU Int. 93 143-50 (Pubitemid 38112985)
    • (2004) BJU International , vol.93 , Issue.1 , pp. 143-150
    • Wu, X.1    Obata, T.2    Khan, Q.3    Highshaw, R.A.4    De Vere White, R.5    Sweeney, C.6
  • 282
    • 3242685291 scopus 로고    scopus 로고
    • Luminal flow induces eNOS activation and translocation in the rat thick ascending limb. II. Role of PI3-kinase and Hsp90
    • DOI 10.1152/ajprenal.00383.2003
    • Ortiz P A, Hong N J and Garvin J L 2004 Luminal flow induces eNOS activation and translocation in the rat thick ascending limb: II. Role of PI3-kinase and Hsp90 Am. J. Physiol. Renal Physiol. 287 F281-8 (Pubitemid 38943945)
    • (2004) American Journal of Physiology - Renal Physiology , vol.287 , Issue.2
    • Ortiz, P.A.1    Hong, N.J.2    Garvin, J.L.3
  • 283
    • 0037294965 scopus 로고    scopus 로고
    • Fluid shear stress inhibits TNF-α-induced apoptosis in osteoblasts: A role for fluid shear stress-induced activation of PI3-kinase and inhibition of caspase-3
    • DOI 10.1002/jcp.10221
    • Pavalko F M, Gerard R L, Ponik S M, Gallagher P J, Jin Y and Norvell S M 2003 Fluid shear stress inhibits TNF-alpha-induced apoptosis in osteoblasts: a role for fluid shear stress-induced activation of PI3-kinase and inhibition of caspase-3 J. Cell. Physiol. 194 194-205 (Pubitemid 36043634)
    • (2003) Journal of Cellular Physiology , vol.194 , Issue.2 , pp. 194-205
    • Pavalko, F.M.1    Gerard, R.L.2    Ponik, S.M.3    Gallagher, P.J.4    Jin, Y.5    Norvell, S.M.6
  • 285
    • 0033105673 scopus 로고    scopus 로고
    • Affinity modulation of very late antigen-5 through phosphatidylinositol 3-kinase in mast cells
    • Kinashi T, Asaoka T, Setoguchi R and Takatsu K 1999 Affinity modulation of very late antigen-5 through phosphatidylinositol 3-kinase in mast cells J. Immunol. 162 2850-7 (Pubitemid 29309311)
    • (1999) Journal of Immunology , vol.162 , Issue.5 , pp. 2850-2857
    • Kinashi, T.1    Asaoka, T.2    Setoguchi, R.3    Takatsu, K.4
  • 286
    • 0031570876 scopus 로고    scopus 로고
    • CD7-Mediated Regulation of Integrin Adhesiveness on Human T Cells Involves Tyrosine Phosphorylation-Dependent Activation of Phosphatidylinositol 3-Kinase
    • Chan A S, Mobley J L, Fields G B and Shimizu Y 1997 CD7-mediated regulation of integrin adhesiveness on human T cells involves tyrosine phosphorylation-dependent activation of phosphatidylinositol 3-kinase J. Immunol. 159 934-42 (Pubitemid 127484248)
    • (1997) Journal of Immunology , vol.159 , Issue.2 , pp. 934-942
    • Chan, A.S.H.1    Mobley, J.L.2    Fields, G.B.3    Shimizu, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.