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Molecular and Cellular Biology
Volumn 34, Issue 3, 2014, Pages 348-361
Grb2 Promotes integrin-induced focal adhesion kinase (FAK) autophosphorylation and directs the phosphorylation of protein tyrosine phosphatase α by the src-FAK kinase complex
Author keywords

[No Author keywords available]
Indexed keywords

DIMER; FOCAL ADHESION KINASE; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; INTEGRIN; MESSENGER RNA; PAXILLIN; PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE ALPHA; TYROSINE; UNCLASSIFIED DRUG;
EID: 84892473800     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00825-13     Document Type: Article
Times cited : (41)
References (55)
  • 1
    • 80053298724 scopus 로고    scopus 로고
    • Molecular architecture and function of matrix adhesions. Cold Spring Harb. Perspect
    • pii a005033
    • Geiger B, Yamada KM. 2011. Molecular architecture and function of matrix adhesions. Cold Spring Harb. Perspect. Biol. 3:pii a005033. http://dx.doi.org/10.1101/cshperspect.a005033.
    • (2011) Biol , vol.3
    • Geiger, B.1    Yamada, K.M.2
  • 3
    • 33744912532 scopus 로고    scopus 로고
    • Regulation of cell adhesion by protein-tyrosine phosphatases. I. Cell-matrix adhesion.
    • Burridge K, Sastry SK, Sallee JL. 2006. Regulation of cell adhesion by protein-tyrosine phosphatases. I. Cell-matrix adhesion. J. Biol. Chem. 281:15593-15596. http://dx.doi.org/10.1074/jbc.R500030200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15593-15596
    • Burridge, K.1    Sastry, S.K.2    Sallee, J.L.3
  • 5
    • 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. http://dx.doi.org/10.1242/jcs.00373.
    • (2003) J. Cell Sci. , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 6
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer DD, Mitra SK, Ilic D. 2004. Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 1692:77- 102. http://dx.doi.org/10.1016/j.bbamcr.2004.04.008.
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 8
    • 0028342938 scopus 로고
    • Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain
    • Xing Z, Chen HC, Nowlen JK, Taylor SJ, Shalloway D, Guan JL. 1994. Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain. Mol. Biol. Cell 5:413-421. http://dx.doi.org/10.1091/mbc.5.4.413.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 413-421
    • Xing, Z.1    Chen, H.C.2    Nowlen, J.K.3    Taylor, S.J.4    Shalloway, D.5    Guan, J.L.6
  • 9
    • 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
  • 10
    • 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 JD, Ruest PJ, Fry DW, Hanks SK. 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. 19:4806-4818.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2    Fry, D.W.3    Hanks, S.K.4
  • 11
    • 0343340035 scopus 로고    scopus 로고
    • Phosphospecific antibodies reveal focal adhesion kinase activation loop phosphorylation in nascent and mature focal adhesions and requirement for the autophosphorylation site
    • Ruest PJ, Roy S, Shi E, Mernaugh RL, Hanks SK. 2000. Phosphospecific antibodies reveal focal adhesion kinase activation loop phosphorylation in nascent and mature focal adhesions and requirement for the autophosphorylation site. Cell Growth Differ. 11:41-48. http://cgd.aacrjournals.org/cgi/content/full/11/1/41.
    • (2000) Cell Growth Differ , vol.11 , pp. 41-48
    • Ruest, P.J.1    Roy, S.2    Shi, E.3    Mernaugh, R.L.4    Hanks, S.K.5
  • 12
    • 79959971564 scopus 로고    scopus 로고
    • Focal adhesion kinase and its signaling pathways in cell migration and angiogenesis
    • Zhao X, Guan JL. 2011. Focal adhesion kinase and its signaling pathways in cell migration and angiogenesis. Adv. Drug Deliv. Rev. 63:610-615. http://dx.doi.org/10.1016/j.addr.2010.11.001.
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 610-615
    • Zhao, X.1    Guan, J.L.2
  • 13
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: in command and control of cell motility
    • Mitra SK, Hanson DA, Schlaepfer DD. 2005. Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6:56-68. http://dx.doi.org/10.1038/nrm1549.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 14
    • 0037437150 scopus 로고    scopus 로고
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages
    • von Wichert G, Jiang G, Kostic A, De Vos K, Sap J, Sheetz MP. 2003. RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages. J. Cell Biol. 161:143-153. http://dx.doi.org/10.1083/jcb.200211061.
    • (2003) J. Cell Biol. , pp. 161-153
    • von Wichert, G.1    Jiang, G.2    Kostic, A.3    De Vos, K.4    Sap, J.5    Sheetz, M.P.6
  • 15
    • 0033587069 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts
    • Su J, Muranjan M, Sap J. 1999. Receptor protein tyrosine phosphatase alpha activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Curr. Biol. 9:505-511. http://dx.doi.org/10.1016/S0960-9822(99)80234-6.
    • (1999) Curr. Biol. , vol.9 , pp. 505-511
    • Su, J.1    Muranjan, M.2    Sap, J.3
  • 16
    • 0037421205 scopus 로고    scopus 로고
    • PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • Zeng L, Si X, Yu WP, Le HT, Ng KP, Teng RM, Ryan K, Wang DZ, Ponniah S, Pallen CJ. 2003. PTP alpha regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J. Cell Biol. 160:137-146. http://dx.doi.org/10.1083/jcb.200206049.
    • (2003) J. Cell Biol. , vol.160 , pp. 137-146
    • Zeng, L.1    Si, X.2    Yu, W.P.3    Le, H.T.4    Ng, K.P.5    Teng, R.M.6    Ryan, K.7    Wang, D.Z.8    Ponniah, S.9    Pallen, C.J.10
  • 17
    • 33744956948 scopus 로고    scopus 로고
    • Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration
    • Chen M, Chen SC, Pallen CJ. 2006. Integrin-induced tyrosine phosphorylation of protein-tyrosine phosphatase-alpha is required for cytoskeletal reorganization and cell migration. J. Biol. Chem. 281:11972-11980. http://dx.doi.org/10.1074/jbc.M600561200.
    • (2006) J. Biol. Chem. , vol.281 , pp. 11972-11980
    • Chen, M.1    Chen, S.C.2    Pallen, C.J.3
  • 18
    • 84866405687 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to position Cas for activation at integrin-mediated focal adhesions
    • Sun G, Cheng SY, Chen M, Lim CJ, Pallen CJ. 2012. Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to position Cas for activation at integrin-mediated focal adhesions. Mol. Cell. Biol. 32:3776- 3789. http://dx.doi.org/10.1128/MCB.00214-12.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 3776-3789
    • Sun, G.1    Cheng, S.Y.2    Chen, M.3    Lim, C.J.4    Pallen, C.J.5
  • 19
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPalpha
    • Zheng XM, Resnick RJ, Shalloway D. 2000. A phosphotyrosine displacement mechanism for activation of Src by PTPalpha.EMBOJ. 19:964-978. http://dx.doi.org/10.1093/emboj/19.5.964.
    • (2000) EMBOJ , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 20
    • 0035503358 scopus 로고    scopus 로고
    • Two mechanisms activate PTPalpha during mitosis
    • Zheng XM, Shalloway D. 2001. Two mechanisms activate PTPalpha during mitosis. EMBO J. 20:6037-6049. http://dx.doi.org/10.1093/emboj/20.21.6037.
    • (2001) EMBO J , vol.20 , pp. 6037-6049
    • Zheng, X.M.1    Shalloway, D.2
  • 21
    • 0028285788 scopus 로고
    • Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo
    • den Hertog J, Tracy S, Hunter T. 1994. Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo. EMBO J. 13:3020-3032.
    • (1994) EMBO J , vol.13 , pp. 3020-3032
    • Den Hertog, J.1    Tracy, S.2    Hunter, T.3
  • 22
    • 0028277776 scopus 로고
    • Receptor tyrosine phosphatase R-PTP-alpha is tyrosine-phosphorylated and associated with the adaptor protein Grb2
    • Su J, Batzer A, Sap J. 1994. Receptor tyrosine phosphatase R-PTP-alpha is tyrosine-phosphorylated and associated with the adaptor protein Grb2. J. Biol. Chem. 269:18731-18734.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18731-18734
    • Su, J.1    Batzer, A.2    Sap, J.3
  • 23
    • 0029949837 scopus 로고    scopus 로고
    • Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains
    • den Hertog J, Hunter T. 1996. Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains. EMBO J. 15:3016-3027.
    • (1996) EMBO J , vol.15 , pp. 3016-3027
    • Den Hertog, J.1    Hunter, T.2
  • 24
    • 0029854844 scopus 로고    scopus 로고
    • Association between receptor proteintyrosine phosphatase RPTPalpha and the Grb2 adaptor Dual Src homology (SH) 2/SH3 domain requirement and functional consequences
    • Su J, Yang LT, Sap J. 1996. Association between receptor proteintyrosine phosphatase RPTPalpha and the Grb2 adaptor. Dual Src homology (SH) 2/SH3 domain requirement and functional consequences. J. Biol. Chem. 271:28086-28096.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28086-28096
    • Su, J.1    Yang, L.T.2    Sap, J.3
  • 25
    • 34547126687 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha stimulates focal adhesion kinase activity required for mitogen-activated kinase-associated interleukin 6 expression
    • Schlaepfer DD, Hou S, Lim ST, Tomar A, Yu H, Lim Y, Hanson DA, Uryu SA, Molina J, Mitra SK. 2007. Tumor necrosis factor-alpha stimulates focal adhesion kinase activity required for mitogen-activated kinase-associated interleukin 6 expression. J. Biol. Chem. 282:17450 - 17459. http://dx.doi.org/10.1074/jbc.M610672200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 17450-17459
    • Schlaepfer, D.D.1    Hou, S.2    Lim, S.T.3    Tomar, A.4    Yu, H.5    Lim, Y.6    Hanson, D.A.7    Uryu, S.A.8    Molina, J.9    Mitra, S.K.10
  • 26
    • 69449103232 scopus 로고    scopus 로고
    • A FAK-p120RasGAPp190RhoGAP complex regulates polarity in migrating cells
    • Tomar A, Lim ST, Lim Y, Schlaepfer DD. 2009. A FAK-p120RasGAPp190RhoGAP complex regulates polarity in migrating cells. J. Cell Sci. 122:1852-1862. http://dx.doi.org/10.1242/jcs.046870.
    • (2009) J. Cell Sci. , vol.122 , pp. 1852-1862
    • Tomar, A.1    Lim, S.T.2    Lim, Y.3    Schlaepfer, D.D.4
  • 27
    • 2642710919 scopus 로고    scopus 로고
    • Physical and functional interactions between receptor-like protein-tyrosine phosphatase alpha and p59fyn
    • Bhandari V, Lim KL, Pallen CJ. 1998. Physical and functional interactions between receptor-like protein-tyrosine phosphatase alpha and p59fyn. J. Biol. Chem. 273:8691-8698. http://dx.doi.org/10.1074/jbc.273.15.8691.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8691-8698
    • Bhandari, V.1    Lim, K.L.2    Pallen, C.J.3
  • 28
    • 68049099370 scopus 로고    scopus 로고
    • Abl knockout differentially affects p130 Crk-associated substrate, vinculin, and paxillin in blood vessels of mice
    • Chen S, Wang R, Li QF, Tang DD. 2009. Abl knockout differentially affects p130 Crk-associated substrate, vinculin, and paxillin in blood vessels of mice. Am. J. Physiol. Heart Circ. Physiol. 297:H533-H539. http://dx.doi.org/10.1152/ajpheart.00237.2009.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Chen, S.1    Wang, R.2    Li, Q.F.3    Tang, D.D.4
  • 29
    • 77953800164 scopus 로고    scopus 로고
    • Grb2 functions at the top of the T-cell antigen receptor-induced tyrosine kinase cascade to control thymic selection
    • Jang IK, Zhang J, Chiang YJ, Kole HK, Cronshaw DG, Zou Y, Gu H. 2010. Grb2 functions at the top of the T-cell antigen receptor-induced tyrosine kinase cascade to control thymic selection. Proc. Natl. Acad. Sci. U. S. A. 107:10620-10625. http://dx.doi.org/10.1073/pnas.0905039107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 10620-10625
    • Jang, I.K.1    Zhang, J.2    Chiang, Y.J.3    Kole, H.K.4    Cronshaw, D.G.5    Zou, Y.6    Gu, H.7
  • 31
    • 84874368710 scopus 로고    scopus 로고
    • Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity
    • Ahmed Z, Lin CC, Suen KM, Melo FA, Levitt JA, Suhling K, Ladbury JE. 2013. Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity. J. Cell Biol. 200:493-504. http://dx.doi.org/10.1083/jcb.201204106.
    • (2013) J. Cell Biol. , vol.200 , pp. 493-504
    • Ahmed, Z.1    Lin, C.C.2    Suen, K.M.3    Melo, F.A.4    Levitt, J.A.5    Suhling, K.6    Ladbury, J.E.7
  • 32
    • 33645214468 scopus 로고    scopus 로고
    • Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA
    • Tsutsumi R, Takahashi A, Azuma T, Higashi H, Hatakeyama M. 2006. Focal adhesion kinase is a substrate and downstream effector of SHP-2 complexed with Helicobacter pylori CagA. Mol. Cell. Biol. 26:261-276. http://dx.doi.org/10.1128/MCB.26.1.261-276.2006.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 261-276
    • Tsutsumi, R.1    Takahashi, A.2    Azuma, T.3    Higashi, H.4    Hatakeyama, M.5
  • 33
    • 84879314654 scopus 로고    scopus 로고
    • The tyrosine phosphatase SHP2 regulates focal adhesion kinase to promote EGF-induced lamellipodia persistence and cell migration
    • Hartman ZR, Schaller MD, Agazie YM. 2013. The tyrosine phosphatase SHP2 regulates focal adhesion kinase to promote EGF-induced lamellipodia persistence and cell migration. Mol. Cancer Res. 11:651-664. http://dx.doi.org/10.1158/1541-7786.MCR-12-0578.
    • (2013) Mol. Cancer Res. , vol.11 , pp. 651-664
    • Hartman, Z.R.1    Schaller, M.D.2    Agazie, Y.M.3
  • 34
    • 0029055784 scopus 로고
    • Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase
    • Hildebrand JD, Schaller MD, Parsons JT. 1995. Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell 6:637-647. http://dx.doi.org/10.1091/mbc.6.6.637.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 637-647
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 35
    • 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. http://dx.doi.org/10.1084/jem.182.4.1089.
    • (1995) J. Exp. Med. , vol.182 , pp. 1089-1099
    • Tachibana, K.1    Sato, T.2    D'Avirro, N.3    Morimoto, C.4
  • 36
    • 30744468126 scopus 로고    scopus 로고
    • Minimal features of paxillin that are required for the tyrosine phosphorylation of focal adhesion kinase
    • Wade R, Vande Pol S. 2006. Minimal features of paxillin that are required for the tyrosine phosphorylation of focal adhesion kinase. Biochem. J. 393:565-573. http://dx.doi.org/10.1042/BJ20051241.
    • (2006) Biochem. J. , vol.393 , pp. 565-573
    • Wade, R.1    Vande Pol, S.2
  • 37
    • 0028609382 scopus 로고
    • Integrinmediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, van der Geer P. 1994. Integrinmediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372:786-791. http://dx.doi.org/10.1038/372786a0.
    • (1994) Nature 372:786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    van der Geer, P.4
  • 38
  • 39
    • 82955248167 scopus 로고    scopus 로고
    • How focal adhesion kinase achieves regulation by linking ligand binding, localization and action
    • Arold ST. 2011. How focal adhesion kinase achieves regulation by linking ligand binding, localization and action. Curr. Opin. Struct. Biol. 21:808- 813. http://dx.doi.org/10.1016/j.sbi.2011.09.008.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 808-813
    • Arold, S.T.1
  • 40
    • 0242495710 scopus 로고    scopus 로고
    • Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction
    • 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. http://dx.doi.org/10.1128/MCB.23.22.8030-8041.2003.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8030-8041
    • Cooper, L.A.1    Shen, T.L.2    Guan, J.L.3
  • 41
    • 34250026140 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of focal adhesion kinase
    • 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. http://dx.doi.org/10.1016/j.cell.2007.05.041.
    • (2007) Cell , vol.129 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 43
    • 79953792614 scopus 로고    scopus 로고
    • Focal adhesion kinase: exploring Fak structure to gain insight into function
    • Hall JE, Fu W, Schaller MD. 2011. Focal adhesion kinase: exploring Fak structure to gain insight into function. Int. Rev. Cell Mol. Biol. 288:185- 225. http://dx.doi.org/10.1016/B978-0-12-386041-5.00005-4.
    • (2011) Int. Rev. Cell Mol. Biol. , vol.288 , pp. 185-225
    • Hall, J.E.1    Fu, W.2    Schaller, M.D.3
  • 44
    • 84863041492 scopus 로고    scopus 로고
    • FAK promotes recruitment of talin to nascent adhesions to control cell motility
    • Lawson C, Lim ST, Uryu S, Chen XL, Calderwood DA, Schlaepfer DD. 2012. FAK promotes recruitment of talin to nascent adhesions to control cell motility. J. Cell Biol. 196:223-232. http://dx.doi.org/10.1083/jcb.201108078.
    • (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
  • 45
    • 0036142219 scopus 로고    scopus 로고
    • The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel M, George EL, Kim A, Tamimi R, Opitz SL, Turner CE, Imamoto A, Thomas SM. 2002. The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 22:901-915. http://dx.doi.org/10.1128/MCB.22.3.901-915.2002.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 901-915
    • Hagel, M.1    George, E.L.2    Kim, A.3    Tamimi, R.4    Opitz, S.L.5    Turner, C.E.6    Imamoto, A.7    Thomas, S.M.8
  • 47
    • 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 MC, Perrotta JA, Turner CE. 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. 135:1109-1123. http://dx.doi.org/10.1083/jcb.135.4.1109.
    • (1996) J. Cell Biol. , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 48
    • 0033579448 scopus 로고    scopus 로고
    • The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin
    • Thomas JW, Cooley MA, Broome JM, Salgia R, Griffin JD, Lombardo CR, Schaller MD. 1999. The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin. J. Biol. Chem. 274: 36684-36692. http://dx.doi.org/10.1074/jbc.274.51.36684.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36684-36692
    • Thomas, J.W.1    Cooley, M.A.2    Broome, J.M.3    Salgia, R.4    Griffin, J.D.5    Lombardo, C.R.6    Schaller, M.D.7
  • 49
    • 0141483200 scopus 로고    scopus 로고
    • Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain
    • Hoellerer MK, Noble ME, Labesse G, Campbell ID, Werner JM, Arold ST. 2003. Molecular recognition of paxillin LD motifs by the focal adhesion targeting domain. Structure 11:1207-1217. http://dx.doi.org/10.1016/j.str.2003.08.010.
    • (2003) Structure , vol.11 , pp. 1207-1217
    • Hoellerer, M.K.1    Noble, M.E.2    Labesse, G.3    Campbell, I.D.4    Werner, J.M.5    Arold, S.T.6
  • 50
    • 34548243624 scopus 로고    scopus 로고
    • Nckbeta adapter controls neuritogenesis by maintaining the cellular paxillin level
    • Guan S, Chen M, Woodley D, Li W. 2007. Nckbeta adapter controls neuritogenesis by maintaining the cellular paxillin level. Mol. Cell. Biol. 27:6001-6011. http://dx.doi.org/10.1128/MCB.01807-06.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6001-6011
    • Guan, S.1    Chen, M.2    Woodley, D.3    Li, W.4
  • 54
    • 24044465136 scopus 로고    scopus 로고
    • Novel Src homology 3 domainbinding motifs identified from proteomic screen of a Pro-rich region
    • Jia CY, Nie J, Wu C, Li C, Li SS. 2005. Novel Src homology 3 domainbinding motifs identified from proteomic screen of a Pro-rich region. Mol. Cell. Proteomics 4:1155-1166. http://dx.doi.org/10.1074/mcp.M500108-MCP200.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1155-1166
    • Jia, C.Y.1    Nie, J.2    Wu, C.3    Li, C.4    Li, S.S.5

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.