Cited by 2,335

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Focal adhesion kinase: in command and control of cell motility.

Mitra, Satyajit K., Hanson, Daniel A., Schlaepfer, David D.·2005·Nature Reviews Molecular Cell Biology

Abstract

A central question in cell biology is how membrane-spanning receptors transmit extracellular signals inside cells to modulate cell adhesion and motility. Focal adhesion kinase (FAK) is a crucial signalling component that is activated by numerous stimuli and functions as a biosensor or integrator to control cell motility. Through multifaceted and diverse molecular connections, FAK can influence the cytoskeleton, structures of cell adhesion sites and membrane protrusions to regulate cell movement.

Overview

Integrity signals

Registry

Crossref · 10.1038/nrm1549

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 3 references

Research works printed but not linked: 123

  1. Brakebusch, C. & Fassler, R. The integrin–actin connection, an eternal love affair. EMBO J. 22, 2324–2333 (2003). · DOI
  2. DeMali, K. A., Wennerberg, K. & Burridge, K. Integrin signaling to the actin cytoskeleton. Curr. Opin. Cell Biol. 15, 572–582 (2003). · DOI
  3. Ridley, A. J. et al. Cell migration: integrating signals from front to back. Science 302, 1704–1709 (2003). · DOI
  4. Parsons, J. T. Focal adhesion kinase: the first ten years. J. Cell Sci. 116, 1409–1416 (2003). Provides a good overview of the early studies on FAK. · DOI
  5. Ilic, D. et al. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377, 539–544 (1995). Shows that null mutation of FAK results in defects in embryonic morphogenesis, and that FAK-null cells show enhanced focal-contact formation and cell motility defects in culture. · DOI
  6. Webb, D. J. et al. FAK–Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nature Cell Biol. 6, 154–161 (2004). · DOI
  7. Palazzo, A. F., Eng, C. H., Schlaepfer, D. D., Marcantonio, E. E. & Gundersen, G. G. Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling. Science 303, 836–839 (2004). Provides evidence that FAK promotes cell polarization through the stabilization of microtubules at leading edges of motile cells. · DOI
  8. Ren, X. et al. Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113, 3673–3678 (2000). · DOI
  9. Agochiya, M. et al. Increased dosage and amplification of the focal adhesion kinase gene in human cancer cells. Oncogene 18, 5646–5653 (1999). · DOI
  10. Bhattacharjee, A. et al. Classification of human lung carcinomas by mRNA expression profiling reveals distinct adenocarcinoma subclasses. Proc. Natl Acad. Sci. USA 98, 13790–13795 (2001). · DOI
  11. Yeoh, E. J. et al. Classification, subtype discovery, and prediction of outcome in pediatric acute lymphoblastic leukemia by gene expression profiling. Cancer Cell 1, 133–143 (2002). · DOI
  12. Cance, W. G. et al. 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, 2417–2423 (2000).
  13. Ilic, D. et al. Focal adhesion kinase is required for blood vessel morphogenesis. Circ. Res. 92, 300–307 (2003). · DOI
  14. Haskell, H. et al. Focal adhesion kinase is expressed in the angiogenic blood vessels of malignant astrocytic tumors in vivo and promotes capillary tube formation of brain microvascular endothelial cells. Clin. Cancer Res. 9, 2157–2165 (2003).
  15. Hauck, C. R., Hsia, D. A., Ilic, D. & Schlaepfer, D. D. v-Src SH3-enhanced interaction with focal adhesion kinase at β1 integrin-containing invadopodia promotes cell invasion. J. Biol. Chem. 277, 12487–12490 (2002). · DOI
  16. Hauck, C. R., Hsia, D. A., Puente, X. S., Cheresh, D. A. & Schlaepfer, D. D. FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth. EMBO J. 21, 6289–6302 (2002). · DOI
  17. Hsia, D. A. et al. Differential regulation of cell motility and invasion by FAK. J. Cell Biol. 160, 753–767 (2003). This reference, together with reference 69, shows that constitutively active Src can bypass the need for FAK in promoting the turnover of focal contacts. · DOI
  18. Schlaepfer, D. D., Mitra, S. K. & Ilic, D. Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 1692, 77–102 (2004). Provides a solid review on the role of FAK during embryonic development. · DOI
  19. Yano, H. et al. Roles played by a subset of integrin signaling molecules in cadherin-based cell–cell adhesion. J. Cell Biol. 166, 283–295 (2004). · DOI
  20. Katsumi, A., Orr, A. W., Tzima, E. & Schwartz, M. A. Integrins in mechanotransduction. J. Biol. Chem. 279, 12001–12004 (2004). · DOI
  21. Carragher, N. O., Westhoff, M. A., Fincham, V. J., Schaller, M. D. & Frame, M. C. A novel role for FAK as a protease-targeting adaptor protein. Regulation by p42 ERK and Src. Curr. Biol. 13, 1442–1450 (2003). · DOI
  22. Hauck, C. R. et al. 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, 7079–7090 (2001).
  23. Sieg, D. J. et al. FAK integrates growth-factor and integrin signals to promote cell migration. Nature Cell Biol. 2, 249–256 (2000). · DOI
  24. Streblow, D. N. et al. Human cytomegalovirus chemokine receptor US28-induced smooth muscle cell migration is mediated by focal adhesion kinase and Src. J. Biol. Chem. 278, 50456–50465 (2003). Together with reference 23, this paper shows that the FAK FERM domain has important roles in promoting growth-factor-stimulated and G-protein-stimulated cell motility. · DOI
  25. Chen, R. et al. Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain. Nature Cell Biol. 3, 439–444 (2001). · DOI
  26. Poullet, P. et al. Ezrin interacts with focal adhesion kinase and induces its activation independently of cell–matrix adhesion. J. Biol. Chem. 276, 37686–37691 (2001). · DOI
  27. Kadare, G. et al. PIAS1-mediated sumoylation of focal adhesion kinase activates its autophosphorylation. J. Biol. Chem. 278, 47434–47440 (2003). Shows that sumoylation of FAK within the FERM domain is associated with catalytic activation and preferential nuclear localization. · DOI
  28. Jones, G. & Stewart, G. Nuclear import of N-terminal FAK by activation of the FcεRI receptor in RBL-2H3 cells. Biochem. Biophys. Res. Comm. 314, 39–45 (2004). · DOI
  29. McKean, D. M. et al. FAK induces expression of Prx1 to promote tenascin-C-dependent fibroblast migration. J. Cell Biol. 161, 393–402 (2003). · DOI
  30. Zhao, J. et al. Identification of transcription factor KLF8 as a downstream target of focal adhesion kinase in its regulation of cyclin D1 and cell cycle progression. Mol. Cell 11, 1503–1515 (2003). · DOI
  31. Hanks, S. K., Ryzhova, L., Shin, N. Y. & Brabek, J. Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front. Biosci. 8, 982–996 (2003). · DOI
  32. Chodniewicz, D. & Klemke, R. L. Regulation of integrin-mediated cellular responses through assembly of a CAS/Crk scaffold. Biochim. Biophys. Acta. 1692, 63–76 (2004). · DOI
  33. Schaller, M. D. Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim. Biophys. Acta. 1540, 1–21 (2001). · DOI
  34. Zhai, J. et al. Direct interaction of focal adhesion kinase with p190RhoGEF. J. Biol. Chem. 278, 24865–24873 (2003). Together with reference 79, shows that FAK can directly activate Rho through binding and phosphorylation of a GEF, and that this activation regulates axonal branching. · DOI
  35. Toutant, M. et al. Alternative splicing controls the mechanisms of FAK autophosphorylation. Mol. Cell. Biol. 22, 7731–7743 (2002). · DOI
  36. Liu, E., Cote, J. F. & Vuori, K. Negative regulation of FAK signaling by SOCS proteins. EMBO J. 22, 5036–5046 (2003). This paper established a link between FAK activation, phosphorylation of Tyr397 and subsequent degradation of FAK. · DOI
  37. Avraham, H., Park, S. Y., Schinkmann, K. & Avraham, S. RAFTK/Pyk2-mediated cellular signalling. Cell. Signal 12, 123–133 (2000). · DOI
  38. Klingbeil, C. K. et al. Targeting Pyk2 to β1-integrin-containing focal contacts rescues fibronectin-stimulated signaling and haptotactic motility defects of focal adhesion kinase-null cells. J. Cell Biol. 152, 97–110 (2001). · DOI
  39. Lim, Y. et al. Phosphorylation of focal adhesion kinase at tyrosine 861 is crucial for Ras transformation of fibroblasts. J. Biol. Chem. 279, 29060–29065 (2004). · DOI
  40. Gabarra-Niecko, V., Keely, P. J. & Schaller, M. D. Characterization of an activated mutant of focal adhesion kinase: 'SuperFAK'. Biochem. J. 365, 591–603 (2002). · DOI
  41. Nowakowski, J. et al. Structures of the cancer-related Aurora-A, FAK, and EphA2 protein kinases from nanovolume crystallography. Structure (Camb.) 10, 1659–1667 (2002). · DOI
  42. Abbi, S. et al. Regulation of focal adhesion kinase by a novel protein inhibitor FIP200. Mol. Biol. Cell 13, 3178–3191 (2002). · DOI
  43. Medley, Q. G. et al. Signaling between focal adhesion kinase and Trio. J. Biol. Chem. 278, 13265–13270 (2003). · DOI
  44. Cooper, L. A., Shen, T. L. & Guan, J. L. Regulation of focal adhesion kinase by its amino-terminal domain through an autoinhibitory interaction. Mol. Cell. Biol. 23, 8030–8041 (2003). · DOI
  45. Zeng, L. et al. PTPα regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J. Cell Biol. 160, 137–146 (2003). · DOI
  46. Chiarugi, P. et al. Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. J. Cell Biol. 161, 933–944 (2003). · DOI
  47. Arias-Salgado, E. G. et al. Src kinase activation by direct interaction with the integrin β cytoplasmic domain. Proc. Natl Acad. Sci. USA 100, 13298–13302 (2003). Shows that selected β-integrin subunits can bind and activate Src in the absence of a contribution from FAK. · DOI
  48. Turner, C. E. Paxillin and focal adhesion signalling. Nature Cell Biol. 2, 231–236 (2000). · DOI
  49. Cho, S. Y. & Klemke, R. L. Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold. J. Cell Biol. 156, 725–736 (2002). · DOI
  50. Brabek, J. et al. CAS promotes invasiveness of Src-transformed cells. Oncogene 23, 7406–7415 (2004). · DOI
  51. Schaller, M. D. Paxillin: a focal adhesion-associated adaptor protein. Oncogene 20, 6459–6472 (2001). · DOI
  52. Subauste, M. C. et al. Vinculin modulation of paxillin–FAK interactions regulates ERK to control survival and motility. J. Cell Biol. 165, 371–381 (2004). · DOI
  53. Hayashi, I., Vuori, K. & Liddington, R. C. The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin. Nature Struct. Biol. 9, 101–106 (2002). · DOI
  54. Liu, G., Guibao, C. D. & Zheng, J. Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase. Mol. Cell. Biol. 22, 2751–2760 (2002). · DOI
  55. Gao, G. et al. 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 (2004). · DOI
  56. Katz, B. Z. et al. Targeting membrane-localized focal adhesion kinase to focal adhesions: roles of tyrosine phosphorylation and SRC family kinases. J. Biol. Chem. 278, 29115–29120 (2003). · DOI
  57. Prutzman, K. C. et al. The focal adhesion targeting domain of focal adhesion kinase contains a hinge region that modulates tyrosine 926 phosphorylation. Structure (Camb.) 12, 881–891 (2004). References 53, 54, 55 and 57 provide structural analyses of the FAK FAT domain and the paxillin LD peptide binding, and show that Tyr925 phosphorylation might require conformational alterations in the FAT domain. · DOI
  58. Ma, A., Richardson, A., Schaefer, E. M. & Parsons, J. T. Serine phosphorylation of focal adhesion kinase in interphase and mitosis: a possible role in modulating binding to p130Cas. Mol. Biol. Cell 12, 1–12 (2001). · DOI
  59. Hunger-Glaser, I., Fan, R. S., Perez-Salazar, E. & Rozengurt, E. PDGF and FGF induce focal adhesion kinase (FAK) phosphorylation at Ser-910: dissociation from Tyr-397 phosphorylation and requirement for ERK activation. J. Cell Physiol. 200, 213–222 (2004). · DOI
  60. Liu, Z. X., Yu, C. F., Nickel, C., Thomas, S. & Cantley, L. G. Hepatocyte growth factor induces ERK-dependent paxillin phosphorylation and regulates paxillin–focal adhesion kinase association. J. Biol. Chem. 277, 10452–10458 (2002). · DOI
  61. Ishibe, S., Joly, D., Zhu, X. & Cantley, L. G. Phosphorylation-dependent paxillin–ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Mol. Cell 12, 1275–1285 (2003). · DOI
  62. Kirchner, J., Kam, Z., Tzur, G., Bershadsky, A. D. & Geiger, B. Live-cell monitoring of tyrosine phosphorylation in focal adhesions following microtubule disruption. J. Cell Sci. 116, 975–986 (2003). · DOI
  63. Zaidel-Bar, R., Ballestrem, C., Kam, Z. & Geiger, B. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J. Cell Sci. 116, 4605–4613 (2003). · DOI
  64. Sieg, D. J., Hauck, C. R. & Schlaepfer, D. D. Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration. J. Cell Sci. 112, 2677–2691 (1999). · DOI
  65. Rajfur, Z., Roy, P., Otey, C., Romer, L. & Jacobson, K. Dissecting the link between stress fibres and focal adhesions by CALI with EGFP fusion proteins. Nature Cell Biol. 4, 286–293 (2002). · DOI
  66. Izaguirre, G. et al. The cytoskeletal/non-muscle isoform of α-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase. J. Biol. Chem. 276, 28676–28685 (2001). · DOI
  67. Yu, D. H., Qu, C. K., Henegariu, O., Lu, X. & Feng, G. S. Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J. Biol. Chem. 273, 21125–21131 (1998). · DOI
  68. Von Wichert, G., Haimovich, B., Feng, G. S. & Sheetz, M. P. Force-dependent integrin–cytoskeleton linkage formation requires downregulation of focal complex dynamics by Shp2. EMBO J. 22, 5023–5035 (2003). Together with reference 67, this study shows that null mutation of SHP2 results in FAK hyperactivation, elevated α-actinin phosphorylation, and the failure to promote the maturation of integrin–cytoskeletal linkages. · DOI
  69. Moissoglu, K. & Gelman, I. H. v-Src rescues actin-based cytoskeletal architecture and cell motility and induces enhanced anchorage independence during oncogenic transformation of focal adhesion kinase-null fibroblasts. J. Biol. Chem. 278, 47946–47959 (2003). · DOI
  70. Visse, R. & Nagase, H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ. Res. 92, 827–839 (2003). · DOI · Paper page
  71. Bhatt, A., Kaverina, I., Otey, C. & Huttenlocher, A. Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain. J. Cell Sci. 115, 3415–3425 (2002). · DOI
  72. Dourdin, N. et al. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J. Biol. Chem. 276, 48382–48388 (2001). · DOI
  73. Cuevas, B. D. et al. MEKK1 regulates calpain-dependent proteolysis of focal adhesion proteins for rear-end detachment of migrating fibroblasts. EMBO J. 22, 3346–3355 (2003). · DOI
  74. Westhoff, M. A., Serrels, B., Fincham, V. J., Frame, M. C. & Carragher, N. O. Src-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling. Mol. Cell. Biol. 24, 8113–8133 (2004). · DOI
  75. Giannone, G. et al. Calcium rises locally trigger focal adhesion disassembly and enhance residency of focal adhesion kinase at focal adhesions. J. Biol. Chem. 279, 28715–28723 (2004). · DOI
  76. Hecker, T. P., Ding, Q., Rege, T. A., Hanks, S. K. & Gladson, C. L. Overexpression of FAK promotes Ras activity through the formation of a FAK/p120RasGAP complex in malignant astrocytoma cells. Oncogene 23, 3962–3971 (2004). · DOI
  77. Chen, B. H., Tzen, J. T., Bresnick, A. R. & Chen, H. C. 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, 33857–33863 (2002). · DOI
  78. Arthur, W. T., Petch, L. A. & Burridge, K. Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10, 719–722 (2000). · DOI
  79. Rico, B. et al. Control of axonal branching and synapse formation by focal adhesion kinase. Nature Neurosci. 7, 1059–1069 (2004). · DOI
  80. Wu, X., Suetsugu, S., Cooper, L. A., Takenawa, T. & Guan, J. L. Focal adhesion kinase regulation of N-WASP subcellular localization and function. J. Biol. Chem. 279, 9565–9576 (2004). · DOI
  81. Palazzo, A. F., Cook, T. A., Alberts, A. S. & Gundersen, G. G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nature Cell Biol. 3, 723–729 (2001). · DOI
  82. Gundersen, G. G., Gomes, E. R. & Wen, Y. Cortical control of microtubule stability and polarization. Curr. Opin. Cell Biol. 16, 106–112 (2004). · DOI
  83. del Pozo, M. A. et al. Integrins regulate Rac targeting by internalization of membrane domains. Science 303, 839–842 (2004). · DOI · Paper page
  84. del Pozo, M. A., Price, L. S., Alderson, N. B., Ren, X. D. & Schwartz, M. A. Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19, 2008–2014 (2000). · DOI
  85. Slack-Davis, J. K. et al. PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK activation. J. Cell Biol. 162, 281–291 (2003). · DOI
  86. Xie, Z. et al. Serine 732 phosphorylation of FAK by Cdk5 is important for microtubule organization, nuclear movement, and neuronal migration. Cell 114, 469–482 (2003). · DOI
  87. Ivankovic-Dikic, I., Gronroos, E., Blaukat, A., Barth, B. -U. & Dikic, I. Pyk2 and FAK regulate neurite outgrowth induced by growth factors and integrins. Nature Cell Biol. 2, 574–581 (2000). · DOI
  88. Calderwood, D. A. Integrin activation. J. Cell Sci. 117, 657–666 (2004). · DOI
  89. Papagrigoriou, E. et al. Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. EMBO J. 23, 2942–2951 (2004). · DOI
  90. Ling, K. et al. Tyrosine phosphorylation of type Iγ phosphatidylinositol phosphate kinase by Src regulates an integrin–talin switch. J. Cell Biol. 163, 1339–1349 (2003). Together with references 91 and 92, this reference shows that FAK–Src phosphorylation events function to control the composition of membrane lipids and the dynamics of focal contacts. · DOI
  91. Wheelock, M. J. & Johnson, K. R. Cadherins as modulators of cellular phenotype. Ann. Rev. Cell Dev. Biol. 19, 207–235 (2003). · DOI
  92. Irby, R. B. & Yeatman, T. J. Increased Src activity disrupts cadherin/catenin-mediated homotypic adhesion in human colon cancer and transformed rodent cells. Cancer Res. 62, 2669–2674 (2002).
  93. Avizienyte, E. et al. Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling. Nature Cell Biol. 4, 632–638 (2002). · DOI
  94. Quadri, S. K., Bhattacharjee, M., Parthasarathi, K., Tanita, T. & Bhattacharya, J. Endothelial barrier strengthening by activation of focal adhesion kinase. J. Biol. Chem. 278, 13342–13349 (2003). · DOI
  95. Miranti, C. K. & Brugge, J. S. Sensing the environment: a historical perspective on integrin signal transduction. Nature Cell Biol. 4, E83–E90 (2002). · DOI
  96. Li, S. et al. The role of the dynamics of focal adhesion kinase in the mechanotaxis of endothelial cells. Proc. Natl Acad. Sci. USA 99, 3546–3551 (2002). · DOI
  97. Wang, H. B., Dembo, M., Hanks, S. K. & Wang, Y. Focal adhesion kinase is involved in mechanosensing during fibroblast migration. Proc. Natl Acad. Sci. USA 98, 11295–11300 (2001). Shows that FAK functions as an important environmental biosensor in promoting directional motility signals in response to changes in substrate flexibility. · DOI
  98. Owen, J. D., Ruest, P. J., Fry, D. W. & Hanks, S. K. 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). · DOI
  99. Cukierman, E., Pankov, R. & Yamada, K. M. Cell interactions with three-dimensional matrices. Curr. Opin. Cell Biol. 14, 633–639 (2002). · DOI
  100. Ilic, D. et al. FAK promotes organization of fibronectin matrix and fibrillar adhesions. J. Cell Sci. 117, 177–187 (2004). · DOI
  101. Beggs, H. E. et al. FAK deficiency in cells contributing to the basal lamina results in cortical abnormalities resembling congenital muscular dystrophies. Neuron 40, 501–514 (2003). References 103 and 104 show that FAK has crucial roles in promoting 3D-matrix assembly and/or remodelling during development and in cell culture model systems. · DOI
  102. Cukierman, E., Pankov, R., Stevens, D. R. & Yamada, K. M. Taking cell–matrix adhesions to the third dimension. Science 294, 1708–1712 (2001). · DOI · Paper page
  103. Xia, H., Nho, R. S., Kahm, J., Kleidon, J. & Henke, C. A. 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 β1 integrin viability signaling pathway. J. Biol. Chem. 279, 33024–33034 (2004). · DOI
  104. Wozniak, M. A., Desai, R., Solski, P. A., Der, C. J. & Keely, P. J. ROCK-generated contractility regulates breast epithelial cell differentiation in response to the physical properties of a three-dimensional collagen matrix. J. Cell Biol. 163, 583–595 (2003). · DOI
  105. Ilic, D. et al. Plasma membrane-associated pY397FAK is a marker of cytotrophoblast invasion in vivo and in vitro. Am. J. Pathol. 159, 93–108 (2001). · DOI
  106. Bowden, E. T., Coopman, P. J. & Mueller, S. C. Invadopodia: unique methods for measurement of extracellular matrix degradation in vitro. Methods Cell Biol. 63, 613–627 (2001). · DOI
  107. Hauck, C. R., Hunter, T. & Schlaepfer, D. D. The v-Src SH3 domain facilitates a cell adhesion-independent association with focal adhesion kinase. J. Biol. Chem. 276, 17653–17662 (2001). · DOI
  108. Stewart, A., Ham, C. & Zachary, I. The focal adhesion kinase amino-terminal domain localises to nuclei and intercellular junctions in HEK 293 and MDCK cells independently of tyrosine 397 and the carboxy-terminal domain. Biochem. Biophys. Res. Comm. 299, 62–73 (2002). · DOI
  109. Chen, H. C., Appeddu, P. A., Isoda, H. & Guan, J. L. Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J. Biol. Chem. 271, 26329–26334 (1996). · DOI
  110. Calderwood, D. A. & Ginsberg, M. H. Talin forges the links between integrins and actin. Nature Cell Biol. 5, 694–697 (2003). · DOI
  111. Zheng, C. et al. Differential regulation of Pyk2 and focal adhesion kinase (FAK). J. Biol. Chem. 273, 2384–2389 (1998). · DOI
  112. Wang, Q. et al. Regulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolin. J. Cell Biol. 160, 565–575 (2003). · DOI
  113. Sieg, D. J. et al. 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, 5933–5947 (1998). · DOI
  114. Lakkakorpi, P. T., Bett, A. J., Lipfert, L., Rodan, G. A. & Duong, L. T. Pyk2 autophosphorylation, but not kinase activity, is necessary for adhesion-induced association with c-Src, osteoclast spreading, and bone resorption. J. Biol. Chem. 278, 11502–11512 (2003). · DOI
  115. Lev, S. et al. Identification of a novel family of targets of Pyk2 related to Drosophila retinal degeneration B (rdgB) protein. Mol. Cell. Biol. 19, 2278–2288 (1999). · DOI
  116. Benbernou, N., Muegge, K. & Durum, S. K. Interleukin (IL)-7 induces rapid activation of Pyk2, which is bound to Janus kinase 1 and IL-7Rα. J. Biol. Chem. 275, 7060–7065 (2000). · DOI
  117. Okigaki, M. et al. Pyk2 regulates multiple signaling events crucial for macrophage morphology and migration. Proc. Natl Acad. Sci. USA 100, 10740–10745 (2003). Shows that null mutation of the FAK-related kinase PYK2 results in integrin and chemokine-stimulated motility defects of macrophages that are not functionally compensated by FAK expression. · DOI
  118. Watson, J. M. et al. Inhibition of the calcium-dependent tyrosine kinase (CADTK) blocks monocyte spreading and motility. J. Biol. Chem. 276, 3536–3542 (2001). · DOI
  119. Guinamard, R., Okigaki, M., Schlessinger, J. & Ravetch, J. V. Absence of marginal zone B cells in Pyk2-deficient mice defines their role in the humoral response. Nature Immunol. 1, 31–36 (2000). · DOI
  120. Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A. & Soriano, P. Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18, 2459–2471 (1999). · DOI
  121. Honda, H. et al. Cardiovascular anomaly, impaired actin bundling and resistance to Src- induced transformation in mice lacking p130Cas. Nature Genet. 19, 361–365 (1998). · DOI
  122. Hagel, M. et al. 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 (2002). · DOI
  123. Xu, W., Baribault, H. & Adamson, E. D. Vinculin knockout results in heart and brain defects during embryonic development. Development 125, 327–337 (1998). · DOI

Cited by

See all 2,335

Metadata

Authors
Mitra, S. K., Hanson, D. A., & Schlaepfer, D. D.
Venue
Nature Reviews Molecular Cell Biology
Published
2005-01-01
Volume
6
Issue
1
Pages
56-68
ISSN
  • 1471-0072
  • 1471-0080
Cited by
2,335
References
3
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: Focal adhesion kinase: in command and control of cell motility. https://app.cochat.ai/papers/10.1038/nrm1549
The paper
Mitra, S. K., Hanson, D. A., & Schlaepfer, D. D. (2005). Focal adhesion kinase: in command and control of cell motility. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm1549