Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases

Molecular and Cellular Biology

Volumn 15, Issue 2, 1995, Pages 954-963

  Calalb, Mihail B ^a   Polte, Thomas R ^a   Hanks, Steven K ^a  

^a VANDERBILT UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE; PROTEIN TYROSINE PHOSPHATASE;

ANIMAL CELL; ANTIGEN ANTIBODY COMPLEX; ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CELL ADHESION; ENZYME ACTIVITY; GENE EXPRESSION; MALIGNANT TRANSFORMATION; MOUSE; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; ROUS SARCOMA ONCOVIRUS; SIGNAL TRANSDUCTION;

ANIMALIA; ONCOVIRINAE; ROUS SARCOMA VIRUS;

EID: 0028877919     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.15.2.954     Document Type: Article

References (49)

1. 2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24). EMBO J. 12:849-859.
2. Boyle, W. J., P. van der Geer, and T. Hunter. 1991. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201:110-149.
3. Burridge, K., K. Fath, T. Kelley, G. Nuckells, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487-525.
4. FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119:893-903.
5. Chen, Q., M. S. Kinch, T. Lin, K. Burridge, and R. L. Juliano. 1994. Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 269:26602-26605.
6. FAK. Mol. Cell. Biol. 14:147-155.
7. src by intermolecular autophosphorylation. Proc. Natl. Acad. Sci. USA 85:4232-4236.
8. De Bondt, H. L., J. Rosenblatt, J. Jancarik, H. D. Jones, D. O. Morgan, and S.-H. Kim. 1993. Crystal structure of cyclin-dependent kinase 2. Nature (London) 363:595-602.
9. Devor, B. B., X. Zhang, S. K. Patel, T. R. Polte, and S. K. Hanks. 1993. Chicken and mouse focal adhesion kinases are similar in structure at their amino-termini. Biochem. Biophys. Res. Commun. 190:1084-1089.
10. Ellis, L., E. Clauser, D. O. Morgan, M. Edery, R. A. Roth, and W. J. Rutter. 1986. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45:721-732.
11. Fesquet, D., J.-C. Labbe, J. Derancourt, J.-P. Capony, S. Galas, F. Girard, T. Lorca, J. Shuttleworth, M. Doree, and J.-C. Cavadore. 1993. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologs. EMBO J. 12:3111-3121.
12. Guan, J. L., and D. Shalloway. 1992. Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature (London) 358:690-692.
13. Guan, J. L., J. E. Trevithick, and R. O. Hynes. 1991. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell Regul. 2:951-964.
14. Hanks, S. K. 1991. Eukaryotic protein kinases. Curr. Opin. Struct. Biol. 1:369-383.
15. Hanks, S. K., M. B. Calalb, M. C. Harper, and S. K. Patel. 1992. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA 89:8487-8491.
16. Hanks, S. K., and T. Hunter. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification based on phylogenetic analysis. In D. G. Hardie and S. K. Hanks (ed.), The protein kinases facts-book, in press. Academic Press, London.
17. Hanks, S. K., A. M. Quinn, and T. Hunter. 1988. The protein kinase family: conserved features and deduced phylogeny of the catalytic domains. Science 241:42-52.
18. Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
19. Hunter, T. 1989. Protein modification: phosphorylation on tyrosine residues. Curr. Opin. Cell Biol. 1:1168-1181.
20. Juliano, R. L., and S. Haskill. 1993. Signal transduction from the extracellular matrix. J. Cell Biol. 120:577-585.
21. Kanner, S. B., A. B. Reynolds, R. R. Vines, and J. T. Parsons. 1990. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc. Natl. Acad. Sci. USA 87:3328-3332.
22. c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49:65-73.
23. Knighton, D. R., J. Zheng, L. F. Tea Eyck, N.-H. Xuong, S. S. Taylor, and J. M. Sowadski. 1991. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253:414-420.
24. Kornberg, L., H. S. Earp, J. T. Parsons, M. Schaller, and R. L. Juliano. 1992. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267:23439-23442.
25. Kornberg, L., H. S. Earp, C. Turner, C. Prokop, and R. L. Juliano. 1991. Signal transduction by integrins: increased protein tyrosine phosphorylation caused clustering of β1 integrins. Proc. Natl. Acad. Sci. USA 88: 8392-8396.
26. FAK in platelets. J. Cell Biol. 119:905-912.
27. Luna, E. J., and A. L. Hitt. 1992. Cytoskeleton-plasma membrane interactions. Science 258:955-964.
28. Maher, P. A., E. B. Pasquale, J. Y. J. Wang, and S. J. Singer. 1985. Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells. Proc. Natl. Acad. Sci. USA 82:6576-6580.
29. Middlemas, D. S., J. Meisenhelder, and T. Hunter. 1994. Identification of TrkB autophosphorylation sites and evidence that phospholipase C-γ1 is a substrate for the TrkB receptor. J. Biol. Chem. 269:5458-5466.
30. Morgan, D. O., and H. L. De Bondt. 1994. Protein kinase regulation: insights from crystal structure analysis. Curr. Opin. Cell Biol. 6:239-246.
31. Payne, D. M., A. J. Rossomando, O. P. Martino, A. K. Erickson, J.-H. Her, J. Shabanowitz, D. F. Hunt, M. J. Weber, and T. W. Sturgill. 1991. Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase). EMBO J. 10:885-892.
32. c-src. Cell 49:75-82.
33. Polte, T. R., A. J. Naftilan, and S. K. Hanks. 1994. Focal adhesion kinase is abundant in developing blood vessels and elevation of its phosphotyrosine content in vascular smooth muscle cells is a rapid response to angiotensin II. J. Cell. Biochem. 55:106-119.
34. cdc2. EMBO J. 12:3123-3132.
35. Schaller, M. D., C. A. Borgman, B. S. Cobb, R. R. Vines, A. B. Reynolds, and J. T. Parsons. 1992. PP125FAK, a structurally unique protein tyrosine kinase associated with focal adhesions. Proc. Natl. Acad. Sci. USA 89:5192-5196.
36. src. Mol. Cell. Biol. 14: 1680-1688.
37. Schlaepfer, D. D., S. K. Hanks, T. Hunter, and P. van der Geer. Nature (London), in press.
38. Schwartz, M. A. 1993. Signaling by integrins: implications for tumorigenesis. Cancer Res. 53:1503-1506.
39. Steinberg, R. A., R. D. Cauthron, M. M. Symcox, and H. Shuntoh. 1993. Autoactivation of catalytic (Cα) subunit of cyclic AMP-dependent protein kinase by phosphorylation of threonine 197. Mol. Cell. Biol. 13:2332-2341.
40. Turner, C. E. 1994. Paxillin: a cytoskeletal target for tyrosine kinases. Bioessays 16:47-52.
41. Tyers, M., G. Tokiwa, R. Nash, and B. Futcher. 1992. The Cln3-Cdc28 kinase complex of S. cerevisiae is regulated by proteolysis and phosphorylation. EMBO J. 11:1773-1781.
42. van der Geer, P., K. Luo, B. M. Sefton, and T. Hunter. 1993. Phosphopeptide mapping and phosphoamino acid analysis on cellulose thin-layer plates, p. 31-59. In D. G. Hardie (ed.). Protein phosphorylation - a practical approach. IRL Press, Oxford.
43. Wigler, M., R. Sweet, G. K. Sim, B. Wold, A. Pellicer, E. Lacy, T. Maniatis, S. Silverstein, and R. Axel. 1979. Transformation of mammalian cells with genes from procaryotes and eucaryotes. Cell 16:777-785.
44. Wilden, P. A., C. R. Kahn, K. Siddle, and M. F. White. 1992. Insulin receptor kinase domain autophosphorylation regulates receptor enzymatic function. J. Biol. Chem. 267:16660-16668.
45. Xing, Z., H.-C. Chen, J. K. Nowlen, S. J. Taylor, D. Shalloway, and J.-L. Guan. 1994. Direct interaction of v-Src with the focal adhesion kinase mediated by the Src SH2 domain. Mol. Biol. Cell 5:413-421.
46. Yu, K.-T., D. K. Werth, I. H. Pastan, and M. P. Czech. 1985. src kinase catalyzes the phosphorylation and activation of the insulin receptor kinase. J. Biol. Chem. 260:5838-5846.
47. Zachary, I., J. Sinnett-Smith, and E. Rozengurt. 1992. Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. J. Biol. Chem. 267:19031-19034.
48. Zhang, F., A. Strand, D. Robbins, M. H. Cobb, and E. J. Goldsmith. 1994. Atomic structure of the MAP kinase ERK2 at 2.3 Å resolution. Nature (London) 367:704-711.
49. Zheng, J., D. R. Knighton, L. F. Ten Eyck, R. Karlsson, N.-H. Xuong, S. S. Taylor, and J. M. Sowadski. 1993. Crystal structure of the catalytic subunit of the cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry 32:2154-2161.