Integrin-mediated signal transduction

Cellular and Molecular Life Sciences

Volumn 54, Issue 6, 1998, Pages 514-526

  Longhurst, C M ^a   Jennings, L K ^a  

^a UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

Author keywords

Cell adhesion; Extracellular matrix; Focal adhesion kinase; Integrin; Signalling

Indexed keywords

INTEGRIN; MEMBRANE PROTEIN;

ARTICLE; CELL DIFFERENTIATION; CELL GROWTH; CELL INTERACTION; CELL MIGRATION; CYTOSKELETON; EXTRACELLULAR MATRIX; HEMOSTASIS; HUMAN; INFLAMMATION; LIGAND BINDING; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION;

CALCIUM; CELL ADHESION MOLECULES; CYTOSKELETON; ENZYME ACTIVATION; FOCAL ADHESION PROTEIN-TYROSINE KINASES; INTEGRINS; MEMBRANE PROTEINS; PHOSPHATIDYLINOSITOLS; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-TYROSINE KINASES; SIGNAL TRANSDUCTION;

EID: 0031814064     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050180     Document Type: Article

References (156)

1. Parise L. V. and Phillips D. R. (1986) Fibronectin-binding properties of the purified platelet glycoprotein IIb-IIIa complex. J. Biol. Chem. 261: 14011-14017
2. Marlin S. D. and Springer T. A. (1987) Purified intercellular adhesion molecule-1 (ICAM-1) is a ligand for lymphocyte function-asociated antigen I (LFA-1). Cell 51: 813-819
3. Bennett J. S. and Vilaire G. (1979) Exposure of platelet fibrinogen receptors by ADP and epinephrine. J. Clin. Invest. 64: 1393-1401
4. 2+ on GPIIb-IIIa interactions with integrilin: enhanced GPIIb-IIIa binding and inhibition of platelet aggregation by reductions in the concentration of ionized calcium in plasma anticoagnlated with citrate. Circulation 96: 1488-1494
5. O'Toole T. E., Loftus J. C., Plow E. F., Glass A. A., Harper J. R. and Ginsberg M. H. (1989) Efficient surface expression of platelet GPIIb-IIIa requires both subunits. Blood 74: 14-18
6. Tuckwell D. S., Brass A. and Humphries M. J. (1992) Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation-binding site. Biochem. J. 285: 325-331
7. Jennings L. and Phillips D. (1982) Purification of glycoprotein IIb and IIIa from human platelet plasma membranes and characterization of a calcium dependent glycoprotein IIb-IIIa complex. J. Biol. Chem. 257: 10458-10466
8. Kieffer N. and Phillips D. R. (1990) Platelet membrane glycoproteins: functions in cellular interactions. Annu. Rev. Cell. Biol. 6: 329-357
9. Tozer E. C., Liddington R. C., Sutcliffe M. J., Smeeton A. H. and Lofus J. C. (1996) Ligand binding to integrin alphaIIb beta 3 is dependent on a MIDAS-like domain in the beta3 subunit. J. Biol. Chem. 271: 21978-21984
10. Hynes R. O. (1992) Integrins: versatility, modulation and signaling in cell adhesion. Cell 69: 11-25
11. Calvete J. J., Mann K., Schaler W., Fernandez-Lafuente R. and Guisan J. M. (1994) Proteolytic degradation of the RGD-binding and non-RGD-binding coiiformers of human platelet integrin glycoprotein IIb IIIa: clues for identification of regions involved in the receptor's activation. Biochem. J. 298: 1-7
12. Rocco M., Spontorno B, and Hantgan R. (1993) Modelling the α IIb/β 3 integrin solution conformation. Protein. Sci. 2: 2154-2166
13. Main A. L., Harvey T. S., Baron M., Boyd J. and Campbell I. D. (1992) The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD mediated interactions. Cell 71: 671-678
14. Obara M., Kang M. and Yamada K. (1988) Site directed mutagenesis of the cell binding domain of human fibronectin: separable, synergistic sites mediate adhesive function. Cell 53: 649-657
15. Bowditch R. D., Halloran C. E., Aota S., Obara M., Plow E. F., Yamada K. M. et al. (1991) Integrin αIIbβ3 (platelet GPIIb-IIIa) recognizes multiple sites in fibronectin. J. Biol. Chem. 266: 23323-23328
16. Fitzgerald L. A. and Phillips D. R. (1985) Calcium regulation of the platelet membrane glycoprotein IIb-IIIa complex. J. Biol. Chem. 260: 11366-11374
17. Gailit J. and Ruoslahti E. (1988) Regulation of the fibronectin receptor affinity by divalent cations. J. Biol. Chem. 263: 12927-12932
18. 2+ dependent binding of a synthetic Arg-Gly-Asp (RGD) peptide to a single site on the purified platelet glycoprotein IIb-IIIa complex. J. Biol. Chem. 264: 13102-13108
19. Ginsberg M. H., Lightsey A., Kunicki T. J., Kaufman A., Marguerie G. A. and Plow E. F. (1986) Divalent cation regulation of the surface orientation of platelet membrane glycoprotein IIb: correlation with fibrinogen binding function and definition of a novel variant of Glanzmann's thrombasthenia. J. Clin. Invest. 78: 1103-1111
20. Frelinger A. L., Lam S. C. T., Plow E. F., Smith M. A., Loftus J. C. and Ginsberg M. H. (1988) Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion. J. Biol. Chem. 263: 12397-12402
21. 58C0(III). Evidence of metal ion coordination sphere involvement in ligand binding. J. Biol. Chem. 266: 11429-11432
22. 2+ binding properties of the platelet glycoprotein IIb ligand-interaction domain. J. Biol. Chem. 267: 1001-1007
23. Irie A., Kamata T., Puzon-McLaughlin W. and Takada Y. (1995) Critical amino acid residues for ligand binding are clustered in a predicted beta-turn of the third N terminal repeat in the integrin alpha 4 and alpha 5 subunits. EMBO J. 14: 5550-5556
24. D'Souza S. E., Ginsberg M. H., Burke T. A. and Plow E. F. (1990) The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its a subunit. J. Biol. Chem. 265: 3440-3446
25. Smith J. W. and Cheresh D. A. (1990) Integrin (αvβ3) ligand interaction. Identification of a heterodimeric RGD binding site on the vitronectin receptor. J. Biol. Chem. 265: 2168-2172
26. D'Souza S. E., Ginsberg M. H., Matsueda G. R. and Plow E. F. (1991) A discrete sequence in a platelet integrin is involved in ligand recognition. Nature 350: 66-68
27. Loftus J. C., O'Toole T. E., Plow E. F., Glass A., Frelinger A. L. and Ginsberg M. H. (1990) A β3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation. Science 249: 915-918
28. D'Souza S. E., Ginsberg M. H., Burke T. A., Lam S. C. and Plow E. F. (1988) Localization of an Arg-Gly-Asp recognition site within an integrin adhesion receptor. Science 242: 91-93
29. Andrieux A., Rabiet M. J., Chapel A., Concord E. and Marguerie G. (1991) A highly conserved sequence of the Arg-Gly-Asp binding domain of the integrin beta-3 subunit is sensitive to stimulation. J. Biol. Chem. 266: 14202-14207
30. D'Souza S. E., Haas T. A., Piotrovicz R. S., Byers-Ward V., McGrath D. E., Soule H. R. et al. (1994) Ligand and cation binding are dual functions of a discrete segment of the β3 integrin: cation displacement is involved in ligand binding. Cell 70: 659-667
31. Bajt M. L. and Loftus J. C. (1994) Mutation of a ligand binding domain of β3 integrin. Integral role of oxygenated residues in αIIbβ3 (GPIIb-IIIa) receptor function. J. Biol. Chem. 269: 20913-20919
32. Charo I., Nannizzi L., Phillips D., Hsu M. and Scarborough R. (1991) Inhibition of fibrinogen binding to GPIIb-IIIa by a GPIIIa peptide. J. Biol. Chem. 266: 1414-1421
33. Lanza F., Stierle A., Fournier D., Morales M., Andre G., Nurden A. T. et al. (1992) A new variant of Glanzmann's Thrombasthenia (Strasbourg I). Platelets with functional defective glycoprotein IIb-IIIa complexes and a glycoprotein IIIa 214Arg-214Trp mutation. J. Clin. Invest. 89: 1995-2004
34. Fournier D., Kabral A., Castaldi P, and Berndt M. (1989) A variant of Glanzmann's thrombasthenia characterized by abnormal glycoprotein IIb IIIa complex formation. Thromb. Haemostas. 62: 977-983
35. Shimizu Y., VanSeventer G. A., Horgan K. J. and Shaw S. (1990) Regulated expression and binding of three VLA (β1) integrin receptors on T cells. Nature 345: 250-253
36. Crowe D., Chui H., Fong S. and Weissman I. (1994) Regulation of the avidity of intesgrin α4β7 by the β7 cyloplasmic domain. J. Biol. Chem. 269: 14411-14418
37. Lollo B. A., Chan K. W. H., Hunson E. M., Moy V. T. and Brian A. A. (1993) Direct evidence for two affinity states for lymphocyte function-associated antigen-1 on activated T cells. J. Biol. Chem. 268: 21693-21700
38. Faull R. J., Kovach N. L., Harlan J. M. and Ginsberg M. H. (1994) Stimulation of integrin-mediated adhesion of T lymphocytes and monocytes: Two mechanisms with divergent biological consequences. J. Exp. Med. 179: 1307-1316
39. Williams M. J., Hughes P. E., O'Toole T. E. and Ginsberg M. H. (1994) The inner world of cell adhesion: integrin cytoplasmic domains. Trends Cell. Biol. 4: 109-112
40. O'Toole T. T., Katagiri Y., Faull R. J., Peter K., Tamura R., Quaranta V. et al. (1994) Integrin cytoplasmic domains mediate inside-out signal trunsduction. J. Cell. Biol. 124: 1047-1059
41. Zhang L. and Plow E. F. (1996) Overlapping but not identical sites are involved in the recognition of C3bi neutrophil inhibitory factor and adhesive ligands by the alphaMbeta2 integrin. J. Biol. Chem. 271: 18211-18216
42. Hotchin N. A. and Hall A. (1995) The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular Rho rac GTPases. J. Cell. Biol. 131: 1857-1865
43. Shattil S. J. and Brass L. F. (1987) Induction of fibrinogen receptor on human platelets by intracellular mediators. J. Biol. Chem. 262: 992-1000
44. Kouns W. C., Wall C. D., White M. M., Fox C. F. and Jennings L. K. (1990) A conformation-dependent epitope of human platelet glycoprotein IIIa. J. Biol. Chem. 265: 20593-20601
45. Heath-Mondoro T., Wall D. C., White M. M. and Jennings L. K. (1996) Selective induction of a glycoprolein IIIa ligand-induced binding site by fibrinoand von Willebrand factor. Blood 88: 3824-3830
46. Jennings L. K., White M. M. and Mandrell T. D. (1995) Interspecies comparison of platelet aggregation, LIBS expression and clot retraction: observed differences in GPIIb-IIIa functional activity. Thromb. Haemost. 74: 1551-1556
47. Hughes P. F., Diaz-Gonzalez F., Leong L., Wu C., McDonald J. A., Shattil S. J. et al. (1996) Breaking the integrin hinge. J. Biol. Chem. 271: 6571-6574
48. Dedhar S. (1994) Novel functions for calreticulin: interaction with integrins and modulation of gene expression? Trends Biochem. Sci. 19: 269-271
49. Coppolino M., Leung-Hegesteijn C., Dedhar S. and Wilkins S. (1995) Inducible interaction of integrin α2β1 with calreticulin: dependence on the activation-state of the integrin. J. Biol. Chem. 270: 23132-23138
50. Gimond C., de Melker A., Aumailley M. and Sonnerberg A. (1995) The cytoplasmic domain of α6A integrin subunit is an in vivo substrate for protein kinase C. Exp. Cell. Res. 216: 232-235
51. Parise L. V., Criss A. B., Nannizzi L. and Wordell M. R. (1990) Glycoprotein IIIa is phosphorylated in intact human platelets. Blood 75: 2363-2368
52. van Willigen G., Hers I., Gorter G. and Akkerman J-W. N. (1996) Exposure of ligand binding sites on platelet integrin αIIbβ3 by phosphorylation of the β3 subunit. Bioehem. J. 314: 769-779
53. Blystone S. D., Lindberg F. P., Williams M. P., McHugh K. P. and Brown E. J. (1996) Inducible tyrosine phosphorylation of β3 integrin requires the αv integrin cytoplasmic tail. J. Biol. Chem. 271: 31458-31462
54. Blystone S. D., Williams M. P., Slater S. E. and Brown E. J. (1997) Requirement of integrin β3 tyrosine 747 for β3 tyrosine phosphorylation and regulation of αvβ3 avidity. J. Biol. Chem. 272: 28757-28761
55. Horwitz A., Duggan K., Buck C., Beckerle M. and Burridge K. (1986) Interaction of plasma fibrinogen receptor with talin. a transmembrane linkage. Nature 320: 531-533
56. Otey C. A., Vasquez G. B., Burridge K. and Erickson B. W. (1993) Mapping of the alpha-actinin binding site within the beta 1 integrin cytoplasmic domain. J. Biol. Chem. 268: 21193-21197
57. Chen Y. P., O'Toole T., Shipley T., Forsyth J., LaFlamme S. E., Yamuda K. M. et al. (1994) Inside-out signal transduetion inhibited by isolated integrin cytoplasmic domains. J. Biol. Chem. 269: 18307-18310
58. Shattil S. J., O'Toole T. E., Eigenthaler M., Thon V., Williams M. H., Babior B. M. et al (1995) β3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin β3 subunit. J. Cell Biol. 131: 807-816
59. Eigenthaler M., Hofferer L., Shattil S. J. and Ginsberg M. H. (1997) A conserved sequence motif in the integrin β3 cytoplasmic domain is required for its specific interaction with β3-endonexin. J. Biol. Chem. 272: 7693-7698
60. Kashiwagi H., Schwartz M. A., Eigenhaler M., Davis K. A., Ginsberg M. H. and Shattil S. J. (1997) Affinity modulation of platelet integrin alphallb beta3 by beta3-endonexin, a selective binding partner of the beta3 integrin cytoplasmic tail. J. Cell. Biol. 137: 1433-1443
61. Naik U. P., Patel P. M. and Parise L. V. (1997) Identification of a novel calcium-binding protein that interacts with integrin αIIb cytoplasmic domain. J. Biol. Chem. 272: 4651-4654
62. Hannigan G. E., Leung-Hagesteijn C., Fitzgibbon L., Coppolino M. G., Radeva G., Filmus J. et al. (1996) Regulation of cell adhesion and anchorage-dependent growth by a new β1 integrin-linked protein kinase. Nature 379: 91-96
63. Hannigan G. E., Bayani J., Weksberg R., Beatty B., Pandita A., Dedhar S. et al. (1997) Mapping of the gene encoding the integrin-linked kinase, ILK. to human chromosome 11p15.5-p15.4. Genomics 42: 177-179
64. Wu C., Keightley S. Y., Leung-Hagesteijn C., Radeva G., Coppolino M., Goicoechea S. et al. (1998) Integrin-linked protein kinase regulates fibronectin matrix assembly, E-cadherin expression, and tumorigenicity. J. Biol. Chem. 273: 528-536
65. Radeva G., Petrocelli T., Leung-Hagesteijn C., Filmus J., Slingerland J. and Dedhar S. (1997) Overexpression of the integrin-linked kinase promotes anchorage-independent cell cycle progression. J. Biol. Chem. 272: 13937-13944
66. Kolanus W., Nagel W., Schiller B., Zeitlmann L., Godar S., Stockinger H. et al. (1996) Alpha L beta 2 integrin LFA-1 binding to ICAM-1 induced by cylohesin-1, a cytoplasmic regulatory molecule. Cell 86: 233-242
67. Burridge K., Turner C. E. and Romer L. H. (1992) Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell. Biol. 118: 893-903
68. Schaller M. D., Otey C. A., Hildebrand J. D. and Parson J. T. (1995) Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J. Cell. Biol. 130: 1181-1187
69. Hildebrand J. D., Schaller M. D. and Parsons J. T. (1993) Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125FAK to cellular focal adhesions. J. Cell. Biol. 123: 993-1005
70. Hildebrand J. D., Schaller M. D. and Parsons J. T. (1995) Paxillin, a tyrosine phosphorylated focal adhesion-associated protein that binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell. 6: 637-647
71. Schaller M. D., Borgman C. A. and Parsons J. T. (1993) Autonomous expression of a noncatalytic domain of focal adhesion associated protein tyrosine kinase pp125FAK. Mol. Cell. Biol. 13: 785-791
72. Richardson A. and Parsons J. T. (1996) A mechanism for regulation of the adhesion associated protein tyrosine kinase pp125FAK. Nature 380: 538-540
73. Richardson A., Shannon J. D., Adams R. B., Schaller M. D. and Parsons J. T. (1997) Identification of integrin-stimtilated sites of serine phosphorylation in FRNK. the separately expressed C-terminal domain of focal adhesion kinase: a potential role for protein kinase A. Biochem. J. 324: 141-149
74. Iiic D., Furuta Y., Kanazawa S., Takeda N., Sobue K., Nakatsuji N. et al. (1995) Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377: 539-544
75. Caalb M. B., Polte T. R. and Hanks S. K. (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
76. Calalb M. B., Zhang X., Polte T. R. and Hanks S. K. (1996) Focal adhesion kinase tyrosine 861 is a major site of phosphorylation by src. Biochem. Biophys. Res. Commun. 228: 662-668
77. Cary L. A., Change J. F. and Guan J. L. (1996) Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J. Cell. Sci. 109: 1787-1794
78. Cobb B. S.. Schaller M. D., Leu T. H. and Parsons J. T. (1994) Stable association of pp60src and pp59fyn with focal adhesion-associated tyrosine kinase, pp125FAK. Mol. Cell. Biol. 14: 147-155
79. Brown M. T. and Cooper J. A. (1996) Regulation substrates and functions of Src. Biochim. Biophys. Acta. 1287: 121-149
80. Hanks S. K. and Polte T. R. (1997) Signaling through focal adhesion kinase. Bioessays 19: 137-144
81. Cooper J. A. and Howell B. (1993) The when and the how of Src regulation. Cell 73: 1051-1054
82. Bergman M., Juokov V., Virtanen I. and Alitalo K. (1995) Overexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreading. Mol. Cell. Biol. 15: 711-722
83. Polte T. R. and Hanks S. K. (1995) Interaction between focal adhesion kinase and crk-associated tyrosine kinase substrate p130cas. Proc. Natl. Acad. Sci. USA 92: 10678-10682
84. Sakai R., Iwamatsu A., Hirano N., Ogawa S., Tanaka T., Mano H. et al. (1994) A novel signaling molecule. p130cas. forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependenl manner. EMBO J. 13: 3748-3756
85. Harte M. T., Hildebrand J. D., Burnham M. R., Bouton A. H. and Parsons JT (1996) p130eas. 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
86. Hamasaki K., Mimura T., Morino N., Furuya H., Nakamoto T., Aizawa S. et al. (1996) Src kinase plays an essential role in integrin mediated tyrosine kinase phosphorylation of crk-assoeiated substrate p130cas. Biochem. Biophys. Res. Commun. 222: 338-343
87. Nakamoto T., Sakai R., Ozawa K., Yazaki Y. and Hirai H. (1996) Direct binding of C- terminal region of p130cas to SH2 and SH3 domains of src kinase. J. Biol. Chem. 271: 8959-8965
88. Lo S. H., Weisberg E. and Chen L. B. (1994) Tensin: a potential link between the cytoskeleton and signal transduction. Bioessays 16: 817-823
89. Schlaepfer D. D. and Hunter T. (1997) Focal adhesion kinase overexpression enhances Ras-dependent integrin signaling to ERK2/mitogen activated protein kinase through interaction with and activation of Src. J. Biol. Chem. 272: 13189-13195
90. Gary L. A., Han D. C., Polte T. R., Hanks S. K. and Guan J.-L. (1998) Identification of p130cas as a mediator of focal adhesion kinase promoted cell migration. J. Cell. Biol. 140: 211-221
91. Bellis S. L., Perrotta J. A., Curtis M. S. and Turner C. E. (1997) Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin. Biochem. J. 325: 375-381
92. Muslin A.J., Tanner J. W., Allen P. M. and Shaw A. S. (1996) Interaction of 14 3-3 with signaling proteins is mediated by the recognition of phosphoserine. Cell 84: 889-897
93. Bellis S. L., Miller J. T. and Turner C. E. (1995) Characterization of tyrosine phosphorylation of paxillin in vitro by-focal adhesion kinase. J. Biol. Chem. 270: 17437-17441
94. Cooray P., Yuan Y., Schoenwaelder S. M., Mitchell C. A., Salem H. H. and Jackson S. P. (1996) Focal adhesion kinase (pp125FAK) cleavage and regulation by calpain. Biochem. J. 318: 41-47
95. Hildebrand J. D., Taylor J. M. and Parsons J. T. (1996) An SH3 domain containing GTPase-activating protein for Rho and cdc42 associates with focal adhesion kinase. Mol. Cell. Biol. 16: 3169-3178
96. Nobes C. D. and Hall A. (1995) Rho, rac and cdc42 GT-Pases regulate the assembly of the multimolecular focal complexes associated with actin stress fibers lamellipodia and filopodia. Cell 81: 53-62
97. 2+ moblization, and the actin cytoskeleton. J. Biol. Chem. 268: 14261-14268
98. Imamura F., Shinkai K., Mukai M., Yoshioka K., Komegome R., Iwasaki T. et al. (1996) Rho-mediated protein tyrosine phosphorylation in lysophosphatidic-acid-induced tumor-cell invasion. Int. J. Cancer 65: 627-632
99. Rankin S., Morii N., Narumiya S. and Rozengurt E. (1994) Botulinium C3 exoenzyme blocks the tyrosine phosphorylation of p125FAK and paxillin induced by bombesin and endothelin. FEBS Lett. 354: 315-319
100. Miyamoto S., Teramoto H., Coso O. A., Gutkind J. S., Burbelo P. D., Akiyama S. K. et al. (1995) Integrin function: molecular hierarchies of cytoskeletal and signaling molecules. J. Cell. Biol. 131: 791-805
101. Miyamoto S., Akiyama S. K. and Yamada K. (1995) Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267: 269-273
102. Burbelo P. C., Miyamoto S., Utani A., Brill S., Yamada K. M., Hall A. et al. (1995) p190-B. a new member of the Rho-GAP family and Rho are induced to cluster after integrin cross-linking. J. Biol. Chem. 270: 30919-30926
103. Zhu X. and Assoian R. K. (1995) Integrin-dependent activation of MAP kinase. a link to shape-dependent cell proliferation. Mol. Biol. Cell. 6: 273-282
104. Schlaepfer D. D. and Hunter T. (1996) Evidence for the in vivo phosphorylation of the Grb2 SH3-domain binding site on focal adhesion kinase by Src-family protein tyrosine kinases. Mol. Biol. Cell. 6: 5623-5633
105. Aspenstrom P., Lindberg U. and Hall A. (1996) Two GT-Pases, cdc42 and Rac bind directly to a protein implicated in immunodeficiency disorder Wiscott-Aldrich syndrome. Curr. Biol. 6: 70-75
106. Symons M., Derry J. M. J., Karlak B., Jiang S., Lematieu V., McCormick F. et al. (1996) Wiscott-Aldrich syndrome protein, a novel effector for the GTPase cdc42, is implicated in actin ploymerization. Cell 84: 723-734
107. Hughes P. E., Renshaw M. W., Pfaff M., Forsyth J., Keivens V. M., Schwartz M. A. et al. (1997) Suppression of integrin activation: a novel function of a Ras Raf-initiated MAP kinase pathway. Cell 88: 521-530
108. Lin T. H., Aplin A. E., Shen Y., Chen Q., Schaller M., Romer L. et al. (1997) Integrin-mediated activation of MAP kinases is independent of FAK: evidence for dual integrin signaling pathways in fibroblasts. J. Cell. Biol. 136: 1385-1395
109. Ridley A. J. and Hall A. (1992) Signal transduction pathways regulating Rho-mediated stress fiber formation: requirement for a tyrosine kinase. EMBO J. 13: 2600-2610
110. Chrzanowska-Wodnicka M. and Burridge K. (1996) Rho stimulated contractibility drives the formation of stress libers and local adhesions. J. Cell. Biol. 133: 1403-1415
111. Hirata K., Kikuchi A., Sasaki T., Kuroda S., Kaibuchi K., Matsuura Y. et al. (1992) Involvement of Rho p21 in the enhanced calcium ion sensitivity of smooth muscle contraction. J. Biol. Chem. 267: 8719-8722
112. Nobes C. D., Hawkins P., Stephens L. and Hall A. (1995) Activation of the small GTP- binding proteins Rho and Rac by growth factor receptors. J. Cell. Sci. 108: 225-233
113. Chong L. D., Traynor-Kaplan A., Bokoch G. M. and Sehwartz M. A. (1994) The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79: 507-513
114. Narumiya S., Ishizaki T. and Watanabe N. (1997) Rho effectors and reorganization of the actin cytoskeleton. FEBS Lett. 410: 68-72
115. Ishizahi T., Maekawa M., Fujisawa K., Okama K., Iwamatsu A., Fijita A. et al. (1996) The small GTP-binding protein Rho binds to and activates a 160kDa Ser Thr protein homologous to myotonic dystrophy kinase. EMBO J. 15: 1885-1893
116. Fujita A., Saito Y., Ishizaki T., Maekawa M., Fujisawa K. and Ushikubi F. (1997) Integrin-dependent translocation of p160ROCK to cytoskeletal complex in thrombin-stimulated human platelets. Biochem. J. 328: 769-775
117. Leung T., Chen X-Q., Manser E. and Lim L. (1996) The p 160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16: 5313-5327
118. Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M. et al. (1996) Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinuse). Science 273: 245-248
119. Pelham R. J. and Wang Y. I. (1997) Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl. Acad. Sci. USA 94: 13661-13665
120. Watanabe N., Maduale P., Reid T., Ishizaki G., Watanabe A., Kakizuhi Y. et al. (1997) p140mDia, a mammalian homolog of drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16: 3044-3056
121. Cao L. G., Babcock G. G., Rubenstein P. A. and Wang Y. (1992) Effects of protilin and profilactin on actin structure and fuction in living cells. J. Cell. Biol. 117: 1023-1029
122. McGlade J., Brunkhorst B., Anderson D., Mbamalu G., Settleman J., Dedhar S, et al. (1993) The amino terminal of GAP regulates cytosketal structure and cell adhesion. EMBO J. 12: 3073-3081
123. McNamee H. P., Ingber D. E. and Schwartz M. A. (1993) Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell. Biol. 121: 673-678
124. Ren X., Bokoch G. M., Traynor-Kaplan A., Jenkins G. H., Anderson R. A. and Schwartz M. A. (1996) Physical association of the small GTPase Rho with a 68 k D phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol. Biol. Cell. 7: 435-442
125. Lassing I. and Lindberg V. (1985) Specific interaction between phosphatidylinositol 4,5-biphosphate. Nature 314: 472-474
126. Janmey P. A. and Stossel T. P. (1987) Modulation of gelsolin function by phosphatidylinositol 4.5-biphosphate. Nature 325: 362-364
127. Stossel T. P. (1989) From signal to pseudopod. J. Biol. Chem. 264: 18261-18264
128. Stossel T. P. (1943) On the crawling of animal cells. Science 260: 1086-1094
129. Fumaki K., Furohashi K., Inagaki M., Endo T., Hatano S. and Takenawa T. (1992) Requirement of phosphatidylinositol 4.5-biphosphale for β-actinin function. Nature 359: 150-152
130. 2 binding proteins involved in signaling by tyrosine kinases. J. Biol. Chem. 269: 1518-1522
131. Gilmore A. P. and Burridge K. (1996) Regulation of vinculin binding to talin and actin by phosphatidylinositol 4,5-biphosphate. Nature 381: 531-535
132. Rana R. S. and Hokin L. E. (1990) Role of phosphoinositides in transmembrane signaling. Physiol. Rev. 70: 115-164
133. Carpenter C. L. and Cantley L. C. (1990) Phosphoinositide kinases. Biochemistry 29: 11147-11156
134. 3. J. Biol. Chem. 269: 32358-32367
135. Zhang J., Fry M. J., Waterfield M. D., Jaken S., Liano L., Fox J. E. B. et al. (1992) Activated phosphatidylinositol 3-kinase associated with membrane cytoskeleton in thrombin exposed platelets. J. Biol. Chem. 267: 4686-4692
136. Chen H.-C. and Guan J.-L. (1994) Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc. Natl. Acad. Sci. USA 91: 10148-10152
137. Welsh G.I., Foulstone E. J., Young S. W., Tavare J.M. and Proud C. G. (1994) Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase. Biochem. J. 303: 15-20
138. Rodriguez-Viciana P., Warne P. H., Dhand R., Vanhaesebroeck B., Gout I., Fry M. J. et al. (1994) Phosphatidylinositol 3-OH kinase as a direct target of Ras. Nature 370: 527-532
139. 2+ signaling. Proc. Natl. Acad. Sci. USA 91: 821-828
140. Savarese D. M., Russell J. T., Fatatis A. and Liotta F. A. (1992) Type IV collagen stimulates an increase in intracellular calcium: potential role in tumor cell motility. J. Biol. Chem. 267: 21928-32195
141. Haimovich B., Kaneshiki N. and Ji P. (1996) Protein kinase C regulates tyrosine phosphorylation of pp125FAK in platelets adherent to fibrinogen. Blood 87: 152-161
142. Dash D., Aepfelbacher M. and Siess W. (1995) The association of pp125FAK pp60Src cdc42Hs and Rap1B with the cytoskeleton of aggregated platelets is a reversible process regulated by calcium. FFBS Lett. 363: 231-234
143. Marks P. W., Hendey B. and Maxfield F. R. (1991) Attachment to fibronectin vitronectin makes human neutrophil migration sensitive to alterations in cytosolic free calcium concentration. J. Cell. Biol. 112: 149-158
144. Hendey B., Klee C. B. and Maxfield F. R (1993) Inhibition of neutrophil chemokinesis on vitronectin by inhibitors of calcinenrin. Science 258: 296-299
145. Sjaastad M. D. and James W. J. (1997) Integrin-mediated calcium signaling and regulation of cell adhesion by intracellular calcium. Bioessays 19: 47-55
146. Maecker H.T., Todd S. C. and Levy S. (1997) The tetraspanin superfamily: molecular facilitators. FASEB J. 11: 428-442
147. Dong J. T., Lamb P. W., Rinker-Schaeffer C. W., Vunkanovic J., Ichikawa T., Issues J. T. et al. (1995) KA11. a metastasis suppressor gene for prostate cancer on human chromosome 11p11.2. Science 268: 884-886
148. Ikeyama S., Koyania M., Yamaoko M., Sasada R. and Miyake M. (1993) Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1 CD9) DNA. J. Exp. Med. 177: 1231-1237
149. Griffith L., Slupsky J., Seehafer J., Boshkov L. and Shaw A. R. (1991) Platelet activation by immobilized monoclonal antibody: evidence for a CD9 proximal signal. Blood 78: 1753-1759
150. Jennings L. K., Fox C. F., Kouns W. C., Mckay C. P., Ballou L. R. and Schultz H. F. (1990) The activation of human platelets mediated by anti-human platelet p24 CD9 monoclonal antibodies. J. Biol. Chem. 265: 3815-3822
151. Slupsky J. R., Cawley J. C., Kaplan C. and Zuzel M. (1997) Analysis of CD9, CD32 and p67 signaling: use of de-granulated platelets indicates a direct involvement of CD9 and p67 in integrin signaling. Br. J. Haematol. 96: 275-286
152. Berditchevski F., Tolias K. F., Wong K., Carpenter C. L. and Hemler M. F. (1997) A novel link between integrins. transmembrane-4 superfamily proteins (CD63 and CD81). and phosphatidylinositol 4-kinase. J. Biol. Chem. 272: 2595-2598
153. Brown E., Hooper I., and Gresham H. (1990) Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins. J. Cell. Biol. 111: 2785-2794
154. Fujimoto T., Fujimura K., Noda M., Takafula T., Shimonuira T. and Kuramoto A. (1995) 50-kD integrin-associaled protein does not detectably influence several functions of glycoprotein IIb-IIIa complex in human platelets. Blood 86: 2174-2182
155. Gao A. G., Lindberg F. P., Finn M. B., Blystone S. D., Brown E. J. and Frazier W. A. (1996) Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin. J. Biol. Chem. 271: 21-24
156. Chung J., Gao A. G. and Frazier W. A. (1997) Thrombospondin acts via integrin-associated protein to activate the platelet integrin alphaIIb beta3. J. Biol. Chem. 272: 14740-14746