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Volumn 22, Issue 7, 2011, Pages 964-975

FAK phosphorylation at Tyr-925 regulates cross-talk between focal adhesion turnover and cell protrusion

Author keywords

[No Author keywords available]

Indexed keywords

FOCAL ADHESION KINASE; PAXILLIN; PROTEIN P130; RAC1 PROTEIN; TYROSINE;

EID: 79953309890     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E10-08-0725     Document Type: Article
Times cited : (112)

References (71)
  • 1
    • 52449089651 scopus 로고    scopus 로고
    • Comparative dynamics of retrograde actin flow and focal adhesions: Formation of nascent adhesions triggers transition from fast to slow flow
    • Alexandrova AY, Arnold K, Schaub S, Vasiliev JM, Meister JJ, Bershadsky AD, Verkhovsky AB (2008). Comparative dynamics of retrograde actin flow and focal adhesions: formation of nascent adhesions triggers transition from fast to slow flow. PloS One 3, e3234.
    • (2008) PloS One , vol.3
    • Alexandrova, A.Y.1    Arnold, K.2    Schaub, S.3    Vasiliev, J.M.4    Meister, J.J.5    Bershadsky, A.D.6    Verkhovsky, A.B.7
  • 2
    • 13944282937 scopus 로고    scopus 로고
    • Identification of Src-specific phosphorylation site on focal adhesion kinase: Dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior
    • DOI 10.1158/0008-5472.CAN-04-1949
    • Brunton VG, Avizienyte E, Fincham VJ, Serrels B, Metcalf CA III, Sawyer TK, Frame MC (2005). Identification of Src-specific phosphorylation site on focal adhesion kinase: dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior. Cancer Res, 65, 1335-1342. (Pubitemid 40270160)
    • (2005) Cancer Research , vol.65 , Issue.4 , pp. 1335-1342
    • Brunton, V.G.1    Avizienyte, E.2    Fincham, V.J.3    Serrels, B.4    Metcalf III, C.A.5    Sawyer, T.K.6    Frame, M.C.7
  • 3
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb MB, Polte TR, Hanks SK (1995). Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol Cell Biol, 15, 954-963.
    • (1995) Mol Cell Biol , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 5
    • 0035830903 scopus 로고    scopus 로고
    • Cleavage of focal adhesion kinase by different proteases during SRC-regulated transformation and apoptosis. Distinct roles for calpain and caspases
    • Carragher NO, Fincham VJ, Riley D, Frame MC (2001). Cleavage of focal adhesion kinase by different proteases during SRC-regulated transformation and apoptosis. Distinct roles for calpain and caspases. J Biol Chem 276, 4270-4275.
    • (2001) J Biol Chem , vol.276 , pp. 4270-4275
    • Carragher, N.O.1    Fincham, V.J.2    Riley, D.3    Frame, M.C.4
  • 6
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src
    • DOI 10.1016/S0960-9822(03)00544-X
    • Carragher NO, Westhoff MA, Fincham VJ, Schaller MD, Frame MC (2003). A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src. Curr Biol 13, 1442-1450. (Pubitemid 37029436)
    • (2003) Current Biology , vol.13 , Issue.16 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 8
    • 33745468872 scopus 로고    scopus 로고
    • Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion
    • Chen SY, Chen HC (2006). Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion. Mol Cell Biol 26, 5155-5167.
    • (2006) Mol Cell Biol , vol.26 , pp. 5155-5167
    • Chen, S.Y.1    Chen, H.C.2
  • 10
    • 33745468872 scopus 로고    scopus 로고
    • Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion
    • Chen SY, Chen HC (2006). Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion. Mol Cell Biol 26, 5155-5167.
    • (2006) Mol Cell Biol , vol.26 , pp. 5155-5167
    • Chen, S.Y.1    Chen, H.C.2
  • 11
    • 51049104617 scopus 로고    scopus 로고
    • Actin and α-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi CK, Vicente-Manzanares M, Zareno J, Whitmore LA, Mogilner A, Horwitz AR (2008). Actin and α-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat Cell Biol 10, 1039-1050.
    • (2008) Nat Cell Biol , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 12
    • 0034490676 scopus 로고    scopus 로고
    • Paxillin binding is not the sole determinant of focal adhesion localization or dominant-negative activity of focal adhesion kinase/focal adhesion kinase-related nonkinase
    • Cooley MA, Broome JM, Ohngemach C, Romer LH, Schaller MD (2000). Paxillin binding is not the sole determinant of focal adhesion localization or dominant-negative activity of focal adhesion kinase/focal adhesion kinase-related nonkinase. Mol Biol Cell 11, 3247-3263. (Pubitemid 32107097)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.9 , pp. 3247-3263
    • Cooley, M.A.1    Broome, J.M.2    Ohngemach, C.3    Romer, L.H.4    Schaller, M.D.5
  • 13
    • 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 LA, Shen TL, Guan JL (2003). Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction. Mol Cell Biol 23, 8030-8041. (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
  • 14
    • 9944258521 scopus 로고    scopus 로고
    • New insights into FAK signaling and localization based on detection of a FAT domain folding intermediate
    • DOI 10.1016/j.str.2004.09.011, PII S0969212604003454
    • Dixon RD, Chen Y, Ding F, Khare SD, Prutzman KC, Schaller MD, Campbell SL, Dokholyan NV (2004). New insights into FAK signaling and localization based on detection of a FAT domain folding intermediate. Structure 12, 2161-2171. (Pubitemid 39593195)
    • (2004) Structure , vol.12 , Issue.12 , pp. 2161-2171
    • Dixon, R.D.S.1    Chen, Y.2    Ding, F.3    Khare, S.D.4    Prutzman, K.C.5    Schaller, M.D.6    Campbell, S.L.7    Dokholyan, N.V.8
  • 16
    • 1842584776 scopus 로고    scopus 로고
    • Newest findings on the oldest oncogene; how activated src does it
    • Frame MC (2004). Newest findings on the oldest oncogene; how activated src does it. J Cell Sci 117, 989-998.
    • (2004) J Cell Sci , vol.117 , pp. 989-998
    • Frame, M.C.1
  • 17
    • 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 KC, King ML, Scheswohl DM, DeRose EF, London RE, Schaller MD, Campbell SL (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, 8441-8451. (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
  • 18
    • 3142619059 scopus 로고    scopus 로고
    • Calcium rises locally trigger focal adhesion disassembly and enhance residency of focal adhesion kinase at focal adhesions
    • DOI 10.1074/jbc.M404054200
    • Giannone G, Ronde P, Gaire M, Beaudouin J, Haiech J, Ellenberg J, Takeda K (2004). Calcium rises locally trigger focal adhesion disassembly and enhance residency of focal adhesion kinase at focal adhesions. J Biol Chem 279, 28715-28723. (Pubitemid 38900156)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28715-28723
    • Giannone, G.1    Ronde, P.2    Gaire, M.3    Beaudouin, J.4    Haiech, J.5    Ellenberg, J.6    Takeda, K.7
  • 19
    • 0037135560 scopus 로고    scopus 로고
    • Calcium oscillations trigger focal adhesion disassembly in human U87 astrocytoma cells
    • DOI 10.1074/jbc.M203952200
    • Giannone G, Ronde P, Gaire M, Haiech J, Takeda K (2002). Calcium oscillations trigger focal adhesion disassembly in human U87 astrocytoma cells. J Biol Chem 277, 26364-26371. (Pubitemid 34967129)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.29 , pp. 26364-26371
    • Giannone, G.1    Ronde, P.2    Gaire, M.3    Haiech, J.4    Takeda, K.5
  • 22
    • 0028951464 scopus 로고
    • Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85α with actin filaments and focal adhesion kinase
    • Guinebault C, Payrastre B, Racaud-Sultan C, Mazarguil H, Breton M, Mauco G, Plantavid M, Chap H (1995). Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85α with actin filaments and focal adhesion kinase. J Cell Biol 129, 831-842.
    • (1995) J Cell Biol , vol.129 , pp. 831-842
    • Guinebault, C.1    Payrastre, B.2    Racaud-Sultan, C.3    Mazarguil, H.4    Breton, M.5    Mauco, G.6    Plantavid, M.7    Chap, H.8
  • 23
    • 33745833345 scopus 로고    scopus 로고
    • Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly
    • DOI 10.1074/jbc.M603508200
    • Guo F, Debidda M, Yang L, Williams DA, Zheng Y (2006). Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly. J Biol Chem 281, 18652-18659. (Pubitemid 44035525)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.27 , pp. 18652-18659
    • Guo, F.1    Debidda, M.2    Yang, L.3    Williams, D.A.4    Zheng, Y.5
  • 24
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal Feedback between Actomyosin and Focal-Adhesion Systems Optimizes Rapid Cell Migration
    • DOI 10.1016/j.cell.2006.05.029, PII S0092867406007197
    • Gupton SL, Waterman-Storer CM (2006). Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125, 1361-1374. (Pubitemid 43929092)
    • (2006) Cell , vol.125 , Issue.7 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 25
    • 27844604200 scopus 로고    scopus 로고
    • Rho GTPases and the control of cell behaviour
    • Hall A (2005). Rho GTPases and the control of cell behaviour. Biochem Soc Trans 33, 891-895.
    • (2005) Biochem Soc Trans , vol.33 , pp. 891-895
    • Hall, A.1
  • 26
    • 27644570788 scopus 로고    scopus 로고
    • Regulation of focal adhesion dynamics and disassembly by phosphorylation of FAK at tyrosine 397
    • DOI 10.1242/jcs.02565
    • Hamadi A, Bouali M, Dontenwill M, Stoeckel H, Takeda K, Ronde P (2005). Regulation of focal adhesion dynamics and disassembly by phosphorylation of FAK at tyrosine 397. J Cell Sci 118, 4415-4425. (Pubitemid 41556340)
    • (2005) Journal of Cell Science , vol.118 , Issue.19 , pp. 4415-4425
    • Hamadi, A.1    Bouali, M.2    Dontenwill, M.3    Stoeckel, H.4    Takeda, K.5    Ronde, P.6
  • 27
    • 59149102148 scopus 로고    scopus 로고
    • Src activation and translocation from focal adhesions to membrane ruffles contribute to formation of new adhesion sites
    • Hamadi A, Deramaudt TB, Takeda K, Ronde P (2009). Src activation and translocation from focal adhesions to membrane ruffles contribute to formation of new adhesion sites. Cell Mol Life Sci 66, 324-338.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 324-338
    • Hamadi, A.1    Deramaudt, T.B.2    Takeda, K.3    Ronde, P.4
  • 28
    • 77956823141 scopus 로고    scopus 로고
    • Hyperphosphorylated FAK delocalizes from focal adhesions to membrane ruffles
    • article 932803
    • Hamadi A, Deramaudt TB, Takeda K, Ronde P (2010). Hyperphosphorylated FAK delocalizes from focal adhesions to membrane ruffles. J Oncol 2010, article 932803.
    • (2010) J Oncol , vol.2010
    • Hamadi, A.1    Deramaudt, T.B.2    Takeda, K.3    Ronde, P.4
  • 29
    • 0029666251 scopus 로고    scopus 로고
    • Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase
    • Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase. J Biol Chem 271, 13649-13655.
    • (1996) J Biol Chem , vol.271 , pp. 13649-13655
    • Harte, M.T.1    Hildebrand, J.D.2    Burnham, M.R.3    Bouton, A.H.4    Parsons, J.T.5
  • 30
    • 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, Liddington RC (2002). The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nat Struct Biol 9, 101-106. (Pubitemid 34132410)
    • (2002) Nature Structural Biology , vol.9 , Issue.2 , pp. 101-106
    • Hayashi, I.1    Vuori, K.2    Liddington, R.C.3
  • 34
    • 3142618052 scopus 로고    scopus 로고
    • Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations
    • DOI 10.1074/jbc.M404114200
    • Kassenbrock CK, Anderson SM (2004). Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations. J Biol Chem 279, 28017-28027. (Pubitemid 38900072)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28017-28027
    • Kassenbrock, C.K.1    Anderson, S.M.2
  • 35
    • 41249086217 scopus 로고    scopus 로고
    • Investigating complexity of protein-protein interactions in focal adhesions
    • Lele TP, Thodeti CK, Pendse J, Ingber DE (2008). Investigating complexity of protein-protein interactions in focal adhesions. Biochem Biophys Res Commun 369, 929-934.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 929-934
    • Lele, T.P.1    Thodeti, C.K.2    Pendse, J.3    Ingber, D.E.4
  • 36
    • 34250026140 scopus 로고    scopus 로고
    • Structural Basis for the Autoinhibition of Focal Adhesion Kinase
    • DOI 10.1016/j.cell.2007.05.041, PII S0092867407006800
    • Lietha D, Cai X, Ceccarelli DF, Li Y, Schaller MD, Eck MJ (2007). Structural basis for the autoinhibition of focal adhesion kinase. Cell 129, 1177-1187. (Pubitemid 46891044)
    • (2007) Cell , vol.129 , Issue.6 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.J.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 37
    • 3142779450 scopus 로고    scopus 로고
    • Phosphorylation of focal adhesion kinase at tyrosine 861 is crucial for ras transformation of fibroblasts
    • DOI 10.1074/jbc.M401183200
    • Lim Y, Han I, Jeon J, Park H, Bahk YY, Oh ES (2004). Phosphorylation of focal adhesion kinase at tyrosine 861 is crucial for Ras transformation of fibroblasts. J Biol Chem 279, 29060-29065. (Pubitemid 38915776)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.28 , pp. 29060-29065
    • Lim, Y.1    Han, I.2    Jeon, J.3    Park, H.4    Bahk, Y.-Y.5    Oh, E.-S.6
  • 38
    • 0035985220 scopus 로고    scopus 로고
    • The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly
    • DOI 10.1091/mbc.E02-01-0018
    • Liu Y, Loijens JC, Martin KH, Karginov AV, Parsons JT (2002). The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly. Mol Biol Cell 13, 2147-2156. (Pubitemid 34651498)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.6 , pp. 2147-2156
    • Liu, Y.1    Loijens, J.C.2    Martin, K.H.3    Karginov, A.V.4    Parsons, J.T.5
  • 41
    • 0024109183 scopus 로고
    • Cytoskeletal dynamics and nerve growth
    • Mitchison T, Kirschner M (1988). Cytoskeletal dynamics and nerve growth. Neuron 1, 761-772.
    • (1988) Neuron , vol.1 , pp. 761-772
    • Mitchison, T.1    Kirschner, M.2
  • 43
    • 0041845333 scopus 로고    scopus 로고
    • ERK 1/2- And JNKs-dependent synthesis of interleukins 6 and 8 by fibroblast-like synoviocytes stimulated with protein I/II, a modulin from oral streptococci, requires focal adhesion kinase
    • DOI 10.1074/jbc.M212065200
    • Neff L, Zeisel M, Druet V, Takeda K, Klein JP, Sibilia J, Wachsmann D (2003). ERK 1/2- and JNKs-dependent synthesis of interleukins 6 and 8 by fibroblast-like synoviocytes stimulated with protein I/II, a modulin from oral streptococci, requires focal adhesion kinase. J Biol Chem 278, 27721-27728. (Pubitemid 36899961)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.30 , pp. 27721-27728
    • Neff, L.1    Zeisel, M.2    Druet, V.3    Takeda, K.4    Klein, J.-P.5    Sibilia, J.6    Wachsmann, D.7
  • 44
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • Parsons JT (2003). Focal adhesion kinase: the first ten years. J Cell Sci 116, 1409-1416.
    • (2003) J Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 45
    • 77949754056 scopus 로고    scopus 로고
    • Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation
    • Pasapera AM, Schneider IC, Rericha E, Schlaepfer DD, Waterman CM (2010). Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation. J Cell Bio 188, 877-890.
    • (2010) J Cell Bio , vol.188 , pp. 877-890
    • Pasapera, A.M.1    Schneider, I.C.2    Rericha, E.3    Schlaepfer, D.D.4    Waterman, C.M.5
  • 46
    • 24744449317 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of VE-cadherin prevents binding of p120- and β-catenin and maintains the cellular mesenchymal state
    • DOI 10.1074/jbc.M505568200
    • Potter MD, Barbero S, Cheresh DA (2005). Tyrosine phosphorylation of VE-cadherin prevents binding of p120- and β-catenin and maintains the cellular mesenchymal state. J Biol Chem 280, 31906-31912. (Pubitemid 41291941)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.36 , pp. 31906-31912
    • Potter, M.D.1    Barbero, S.2    Cheresh, D.A.3
  • 47
    • 2342649951 scopus 로고    scopus 로고
    • The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation
    • DOI 10.1016/j.str.2004.02.028, PII S0969212604000978
    • Prutzman KC, Gao G, King ML, Iyer VV, Mueller GA, Schaller MD, Campbell SL (2004). The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation. Structure 12, 881-891. (Pubitemid 38595776)
    • (2004) Structure , vol.12 , Issue.5 , pp. 881-891
    • Prutzman, K.C.1    Gao, G.2    King, M.L.3    Iyer, V.V.4    Mueller, G.A.5    Schaller, M.D.6    Campbell, S.L.7
  • 48
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, Parsons JT (1994). Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 14, 1680-1688.
    • (1994) Mol Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 49
    • 0028986116 scopus 로고
    • pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller MD, Parsons JT (1995). pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol Cell Biol 15, 2635-2645.
    • (1995) Mol Cell Biol , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 50
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, Van Der Geer P (1994). Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372, 786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 51
    • 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 DD, 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, 5623-5633. (Pubitemid 26315082)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.10 , pp. 5623-5633
    • Schlaepfer, D.D.1    Hunter, T.2
  • 52
    • 0842281489 scopus 로고    scopus 로고
    • Multiple connections link FAK to cell motility and invasion
    • DOI 10.1016/j.gde.2003.12.002
    • Schlaepfer DD, Mitra SK (2004). Multiple connections link FAK to cell motility and invasion. Curr Opin Genet Dev 14, 92-101. (Pubitemid 38167483)
    • (2004) Current Opinion in Genetics and Development , vol.14 , Issue.1 , pp. 92-101
    • Schlaepfer, D.D.1    Mitra, S.K.2
  • 54
    • 33745245543 scopus 로고    scopus 로고
    • Integrating Adhesion, Protrusion, and Contraction during Cell Migration
    • DOI 10.1016/j.cell.2006.06.015, PII S0092867406007732
    • Schwartz MA, Horwitz AR (2006). Integrating adhesion, protrusion, and contraction during cell migration. Cell 125, 1223-1225. (Pubitemid 43929100)
    • (2006) Cell , vol.125 , Issue.7 , pp. 1223-1225
    • Schwartz, M.A.1    Horwitz, A.R.2
  • 55
    • 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 VG, Holt M, McLean GW, Gray CH, Jones GE, Frame MC (2007). Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. Nat Cell Biol 9, 1046-1056. (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
  • 56
    • 53149139896 scopus 로고    scopus 로고
    • Phosphorylation of p130Cas initiates Rac activation and membrane ruffling
    • Sharma A, Mayer BJ (2008). Phosphorylation of p130Cas initiates Rac activation and membrane ruffling. BMC Cell Biol 9, 50.
    • (2008) BMC Cell Biol , vol.9 , pp. 50
    • Sharma, A.1    Mayer, B.J.2
  • 58
    • 0032820782 scopus 로고    scopus 로고
    • Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration
    • Sieg DJ, Hauck CR, Schlaepfer DD (1999). Required role of focal adhesion kinase, (FAK) for integrin-stimulated cell migration. J Cell Sci 112, 2677-2691. (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
  • 59
    • 0028980418 scopus 로고
    • Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK
    • Tachibana K, Sato T, D'Avirro N, Morimoto C (1995). Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. J Exp Med 182, 1089-1099.
    • (1995) J Exp Med , vol.182 , pp. 1089-1099
    • Tachibana, K.1    Sato, T.2    D'Avirro, N.3    Morimoto, C.4
  • 60
    • 0030669961 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates
    • DOI 10.1074/jbc.272.46.29083
    • Tachibana K, Urano T, Fujita H, Ohashi Y, Kamiguchi K, Iwata S, Hirai H, Morimoto C (1997). Tyrosine phosphorylation of Crk-associated substrates by focal adhesion kinase. A putative mechanism for the integrin-mediated tyrosine phosphorylation of Crk-associated substrates. J Biol Chem 272, 29083-29090. (Pubitemid 27498196)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.46 , pp. 29083-29090
    • Tachibana, K.1    Urano, T.2    Fujitat, H.3    Ohashi, Y.4    Kamiguchi, K.5    Iwata, S.6    Hirai, H.7    Morimoto, C.8
  • 63
    • 0034941053 scopus 로고    scopus 로고
    • c-srcand related tyrosine kinases: A role in the assembly and reorganization of matrix adhesions
    • Volberg T, Romer L, Zamir E, Geiger B (2001). pp60(c-src) and related tyrosine kinases: a role in the assembly and reorganization of matrix adhesions. J Cell Sci 114, 2279-2289. (Pubitemid 32633699)
    • (2001) Journal of Cell Science , vol.114 , Issue.12 , pp. 2279-2289
    • Volberg, T.1    Romer, L.2    Zamir, E.3    Geiger, B.4
  • 66
    • 4444338326 scopus 로고    scopus 로고
    • Src-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling
    • DOI 10.1128/MCB.24.18.8113-8133.2004
    • Westhoff MA, Serrels B, Fincham VJ, Frame MC, Carragher NO (2004). SRC-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling. Mol Cell Biol 24, 8113-8133. (Pubitemid 39167461)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.18 , pp. 8113-8133
    • Westhoff, M.A.1    Serrels, B.2    Fincham, V.J.3    Frame, M.C.4    Carragher, N.O.5
  • 68
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • DOI 10.1074/jbc.273.33.21125
    • Yu DH, Qu CK, Henegariu O, Lu X, Feng GS (1998). Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J Biol Chem 273, 21125-21131. (Pubitemid 28385400)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 21125-21131
    • Yu, D.-H.1    Qu, C.-K.2    Henegariu, O.3    Lu, X.4    Feng, G.-S.5
  • 69
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • DOI 10.1242/jcs.00792
    • Zaidel-Bar R, Ballestrem C, Kam Z, Geiger B (2003). Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J Cell Sci 116, 4605-4613. (Pubitemid 37461615)
    • (2003) Journal of Cell Science , vol.116 , Issue.22 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 71
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • DOI 10.1242/jcs.03314
    • Zaidel-Bar R, Milo R, Kam Z, Geiger B (2007b). A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J Cell Sci 120, 137-148. (Pubitemid 46206656)
    • (2007) Journal of Cell Science , vol.120 , Issue.1 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4


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