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Volumn 111, Issue 31, 2014, Pages

Phosphatidylinositol 4,5-bisphosphate triggers activation of focal adhesion kinase by inducing clustering and conformational changes

Author keywords

Cell signaling; Phosphoinositides

Indexed keywords

EZRIN; FOCAL ADHESION KINASE; INTEGRIN; MOESIN; PHOSPHATIDYLINOSITOL 4 PHOSPHATE 5 KINASE TYPE 1GAMMA; PHOSPHATIDYLINOSITOL 4 PHOSPHATE KINASE; RADIXIN; UNCLASSIFIED DRUG;

EID: 84905666209     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1317022111     Document Type: Article
Times cited : (116)

References (48)
  • 1
    • 84878541453 scopus 로고    scopus 로고
    • Mechanosensitivity and compositional dynamics of cell-matrix adhesions
    • Schiller HB, Fässler R (2013) Mechanosensitivity and compositional dynamics of cell-matrix adhesions. EMBO Rep 14(6):509-519.
    • (2013) EMBO Rep , vol.14 , Issue.6 , pp. 509-519
    • Schiller, H.B.1    Fässler, R.2
  • 2
    • 77951184829 scopus 로고    scopus 로고
    • Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions
    • Schaller MD (2010) Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions. J Cell Sci 123(Pt 7):1007-1013.
    • (2010) J Cell Sci , vol.123 , Issue.PART 7 , pp. 1007-1013
    • Schaller, M.D.1
  • 3
    • 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(8):610-615.
    • (2011) Adv Drug Deliv Rev , vol.63 , Issue.8 , pp. 610-615
    • Zhao, X.1    Guan, J.L.2
  • 4
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir E, Geiger B (2001) Molecular complexity and dynamics of cell-matrix adhesions. J Cell Sci 114(Pt 20):3583-3590. (Pubitemid 33041040)
    • (2001) Journal of Cell Science , vol.114 , Issue.20 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 5
    • 77955587900 scopus 로고    scopus 로고
    • Focal adhesion kinase is required for intestinal regeneration and tumorigenesis downstream of Wnt/c-Myc signaling
    • Ashton GH, et al. (2010) Focal adhesion kinase is required for intestinal regeneration and tumorigenesis downstream of Wnt/c-Myc signaling. Dev Cell 19(2):259-269.
    • (2010) Dev Cell , vol.19 , Issue.2 , pp. 259-269
    • Ashton, G.H.1
  • 6
    • 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
    • Lim ST, et al. (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(28):21526-21536.
    • (2010) J Biol Chem , vol.285 , Issue.28 , pp. 21526-21536
    • Lim, S.T.1
  • 8
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilić D, et al. (1995) Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377(6549):539-544.
    • (1995) Nature , vol.377 , Issue.6549 , pp. 539-544
    • Ilić, D.1
  • 9
    • 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
    • Chen BH, Tzen JT, Bresnick AR, Chen HC (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(37):33857-33863.
    • (2002) J Biol Chem , vol.277 , Issue.37 , pp. 33857-33863
    • Chen, B.H.1    Tzen, J.T.2    Bresnick, A.R.3    Chen, H.C.4
  • 10
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren XD, et al. (2000) Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J Cell Sci 113(Pt 20):3673-3678.
    • (2000) J Cell Sci , vol.113 , Issue.PART 20 , pp. 3673-3678
    • Ren, X.D.1
  • 11
    • 70349332774 scopus 로고    scopus 로고
    • Focal adhesion kinase: Switching between GAPs and GEFs in the regulation of cell motility
    • Tomar A, Schlaepfer DD (2009) Focal adhesion kinase: Switching between GAPs and GEFs in the regulation of cell motility. Curr Opin Cell Biol 21(5):676-683.
    • (2009) Curr Opin Cell Biol , vol.21 , Issue.5 , pp. 676-683
    • Tomar, A.1    Schlaepfer, D.D.2
  • 12
    • 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 RW, Parsons JT (2008) Focal adhesion kinase as a regulator of cell tension in the progression of cancer. Semin Cancer Biol 18(1):45-52. (Pubitemid 350266368)
    • (2008) Seminars in Cancer Biology , vol.18 , Issue.1 , pp. 45-52
    • Tilghman, R.W.1    Parsons, J.T.2
  • 14
    • 67651085772 scopus 로고    scopus 로고
    • Signal transduction by focal adhesion kinase in cancer
    • Zhao J, Guan JL (2009) Signal transduction by focal adhesion kinase in cancer. Cancer Metastasis Rev 28(1-2):35-49.
    • (2009) Cancer Metastasis Rev , vol.28 , Issue.1-2 , pp. 35-49
    • Zhao, J.1    Guan, J.L.2
  • 15
    • 38949089708 scopus 로고    scopus 로고
    • Focal adhesion kinase: Targeting adhesion signaling pathways for therapeutic intervention
    • DOI 10.1158/1078-0432.CCR-07-2220
    • Parsons JT, Slack-Davis J, Tilghman R, Roberts WG (2008) Focal adhesion kinase: Targeting adhesion signaling pathways for therapeutic intervention. Clin Cancer Res 14(3):627-632. (Pubitemid 351231140)
    • (2008) Clinical Cancer Research , vol.14 , Issue.3 , pp. 627-632
    • Parsons, J.T.1    Slack-Davis, J.2    Tilghman, R.3    Roberts, W.G.4
  • 16
    • 77952469195 scopus 로고    scopus 로고
    • Therapeutic potential and limitations of new FAK inhibitors in the treatment of cancer
    • Schultze A, Fiedler W (2010) Therapeutic potential and limitations of new FAK inhibitors in the treatment of cancer. Expert Opin Investig Drugs 19(6):777-788.
    • (2010) Expert Opin Investig Drugs , vol.19 , Issue.6 , pp. 777-788
    • Schultze, A.1    Fiedler, W.2
  • 17
    • 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 ST, Hoellerer MK, Noble ME (2002) The structural basis of localization and signaling by the focal adhesion targeting domain. Structure 10(3):319-327. (Pubitemid 34230620)
    • (2002) Structure , vol.10 , Issue.3 , pp. 319-327
    • Arold, S.T.1    Hoellerer, M.K.2    Noble, M.E.M.3
  • 19
    • 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(2):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
  • 20
    • 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(22):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
  • 21
    • 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, et al. (2007) Structural basis for the autoinhibition of focal adhesion kinase. Cell 129(6):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
  • 22
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller MD, et al. (1994) Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 14(3):1680-1688.
    • (1994) Mol Cell Biol , vol.14 , Issue.3 , pp. 1680-1688
    • Schaller, M.D.1
  • 24
    • 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(2):954-963.
    • (1995) Mol Cell Biol , vol.15 , Issue.2 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 25
    • 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(5):2635-2645.
    • (1995) Mol Cell Biol , vol.15 , Issue.5 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 26
    • 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, et al. (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(46):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
  • 28
    • 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(13):5155-5167.
    • (2006) Mol Cell Biol , vol.26 , Issue.13 , pp. 5155-5167
    • Chen, S.Y.1    Chen, H.C.2
  • 29
    • 79955783528 scopus 로고    scopus 로고
    • Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism
    • Plaza-Menacho I, et al. (2011) Focal adhesion kinase (FAK) binds RET kinase via its FERM domain, priming a direct and reciprocal RET-FAK transactivation mechanism. J Biol Chem 286(19):17292-17302.
    • (2011) J Biol Chem , vol.286 , Issue.19 , pp. 17292-17302
    • Plaza-Menacho, I.1
  • 30
    • 0033772308 scopus 로고    scopus 로고
    • FAK integrates growth-factor and integrin signals to promote cell migration
    • Sieg DJ, et al. (2000) FAK integrates growth-factor and integrin signals to promote cell migration. Nat Cell Biol 2(5):249-256.
    • (2000) Nat Cell Biol , vol.2 , Issue.5 , pp. 249-256
    • Sieg, D.J.1
  • 31
    • 37549060016 scopus 로고    scopus 로고
    • Spatial and temporal regulation of focal adhesion kinase activity in living cells
    • Cai X, et al. (2008) Spatial and temporal regulation of focal adhesion kinase activity in living cells. Mol Cell Biol 28(1):201-214.
    • (2008) Mol Cell Biol , vol.28 , Issue.1 , pp. 201-214
    • Cai, X.1
  • 32
    • 46149093439 scopus 로고    scopus 로고
    • Structural Basis for the Autoinhibition of Talin in Regulating Integrin Activation
    • DOI 10.1016/j.molcel.2008.06.011, PII S1097276508004292
    • Goksoy E, et al. (2008) Structural basis for the autoinhibition of talin in regulating integrin activation. Mol Cell 31(1):124-133. (Pubitemid 351905930)
    • (2008) Molecular Cell , vol.31 , Issue.1 , pp. 124-133
    • Goksoy, E.1    Ma, Y.-Q.2    Wang, X.3    Kong, X.4    Perera, D.5    Plow, E.F.6    Qin, J.7
  • 33
    • 65449131260 scopus 로고    scopus 로고
    • Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini
    • Palmer SM, Playford MP, Craig SW, Schaller MD, Campbell SL (2009) Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini. J Biol Chem 284(11):7223-7231.
    • (2009) J Biol Chem , vol.284 , Issue.11 , pp. 7223-7231
    • Palmer, S.M.1    Playford, M.P.2    Craig, S.W.3    Schaller, M.D.4    Campbell, S.L.5
  • 34
    • 81255134470 scopus 로고    scopus 로고
    • Integrin adhesion and force coupling are independently regulated by localized PtdIns(4,5)2 synthesis
    • Legate KR, et al. (2011) Integrin adhesion and force coupling are independently regulated by localized PtdIns(4,5)2 synthesis. EMBO J 30(22):4539-4553.
    • (2011) EMBO J , vol.30 , Issue.22 , pp. 4539-4553
    • Legate, K.R.1
  • 35
    • 0029872178 scopus 로고    scopus 로고
    • Integrin-dependent control of inositol lipid synthesis in vascular endothelial cells and smooth muscle cells
    • DOI 10.1006/excr.1996.0118
    • McNamee HP, Liley HG, Ingber DE (1996) Integrin-dependent control of inositol lipid synthesis in vascular endothelial cells and smooth muscle cells. Exp Cell Res 224(1):116-122. (Pubitemid 26116895)
    • (1996) Experimental Cell Research , vol.224 , Issue.1 , pp. 116-122
    • Mcnamee, H.P.1    Liley, H.G.2    Ingber, D.E.3
  • 37
    • 0037038412 scopus 로고    scopus 로고
    • Type Igamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • DOI 10.1038/nature01082
    • Ling K, Doughman RL, Firestone AJ, Bunce MW, Anderson RA (2002) Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 420(6911):89-93. (Pubitemid 35291445)
    • (2002) Nature , vol.420 , Issue.6911 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 38
    • 70149098505 scopus 로고    scopus 로고
    • Coarse-grained modeling of allosteric regulation in protein receptors
    • Balabin IA, Yang W, Beratan DN (2009) Coarse-grained modeling of allosteric regulation in protein receptors. Proc Natl Acad Sci USA 106(34):14253-14258.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.34 , pp. 14253-14258
    • Balabin, I.A.1    Yang, W.2    Beratan, D.N.3
  • 39
    • 84878258238 scopus 로고    scopus 로고
    • Platelets lacking PIP5KIγ have normal integrin activation but impaired cytoskeletal-membrane integrity and adhesion
    • Wang Y, et al. (2013) Platelets lacking PIP5KIγ have normal integrin activation but impaired cytoskeletal-membrane integrity and adhesion. Blood 121(14):2743-2752.
    • (2013) Blood , vol.121 , Issue.14 , pp. 2743-2752
    • Wang, Y.1
  • 40
    • 78649483796 scopus 로고    scopus 로고
    • Nanoscale architecture of integrin-based cell adhesions
    • Kanchanawong P, et al. (2010) Nanoscale architecture of integrin-based cell adhesions. Nature 468(7323):580-584.
    • (2010) Nature , vol.468 , Issue.7323 , pp. 580-584
    • Kanchanawong, P.1
  • 41
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J (2000) Cell signaling by receptor tyrosine kinases. Cell 103(2):211-225.
    • (2000) Cell , vol.103 , Issue.2 , pp. 211-225
    • Schlessinger, J.1
  • 42
    • 84897862926 scopus 로고    scopus 로고
    • FAK dimerization controls its kinase-dependent functions at focal adhesions
    • Brami-Cherrier K, et al. (2014) FAK dimerization controls its kinase-dependent functions at focal adhesions. EMBO J 33(4):356-370.
    • (2014) EMBO J , vol.33 , Issue.4 , pp. 356-370
    • Brami-Cherrier, K.1
  • 44
    • 84876000745 scopus 로고    scopus 로고
    • Visualizing and manipulating focal adhesion kinase regulation in live cells
    • Ritt M, Guan JL, Sivaramakrishnan S (2013) Visualizing and manipulating focal adhesion kinase regulation in live cells. J Biol Chem 288(13):8875-8886.
    • (2013) J Biol Chem , vol.288 , Issue.13 , pp. 8875-8886
    • Ritt, M.1    Guan, J.L.2    Sivaramakrishnan, S.3
  • 45
    • 0030049479 scopus 로고    scopus 로고
    • Pre-steady-state kinetic analysis of cAMP-dependent protein kinase using rapid quench flow techniques
    • DOI 10.1021/bi952144+
    • Grant BD, Adams JA (1996) Pre-steady-state kinetic analysis of cAMP-dependent protein kinase using rapid quench flow techniques. Biochemistry 35(6):2022-2029. (Pubitemid 26062652)
    • (1996) Biochemistry , vol.35 , Issue.6 , pp. 2022-2029
    • Grant, B.D.1    Adams, J.A.2
  • 47
    • 78651401021 scopus 로고    scopus 로고
    • Phosphorylation of focal adhesion kinase on tyrosine 194 by Met leads to its activation through relief of autoinhibition
    • Chen TH, Chan PC, Chen CL, Chen HC (2011) Phosphorylation of focal adhesion kinase on tyrosine 194 by Met leads to its activation through relief of autoinhibition. Oncogene 30(2):153-166.
    • (2011) Oncogene , vol.30 , Issue.2 , pp. 153-166
    • Chen, T.H.1    Chan, P.C.2    Chen, C.L.3    Chen, H.C.4
  • 48
    • 34447504018 scopus 로고    scopus 로고
    • Type Igamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration
    • DOI 10.1083/jcb.200701078
    • Sun Y, Ling K, Wagoner MP, Anderson RA (2007) Type I gamma phosphatidylinositol phosphate kinase is required for EGF-stimulated directional cell migration. J Cell Biol 178(2):297-308. (Pubitemid 47076465)
    • (2007) Journal of Cell Biology , vol.178 , Issue.2 , pp. 297-308
    • Sun, Y.1    Ling, K.2    Wagoner, M.P.3    Anderson, R.A.4


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