Role of focal adhesion proteins in signal transduction and oncogenesis

Critical Reviews in Oncogenesis

Volumn 8, Issue 4, 1997, Pages 343-358

  Weisberg, Ellen ^a   Sattler, Martin ^b   Ewaniuk, Darren S ^b   Salgia, Ravi ^b,c  

^a HARVARD MEDICAL SCHOOL   (United States)

^b DANA FARBER CANCER INSTITUTE   (United States)

^c BRIGHAM AND WOMEN S HOSPITAL   (United States)

Author keywords

BCR ABL; Cell motility; Focal adhesion; Integrin; P125(FAK); Paxillin; Rho; Src; Tensin

Indexed keywords

ALPHA INTERFERON; GUANINE NUCLEOTIDE BINDING PROTEIN; INTEGRIN; ONCOPROTEIN; PAXILLIN; TENSIN; UNCLASSIFIED DRUG;

ARTICLE; CARCINOGENESIS; CELL ADHESION; CELL MOTILITY; CELL TRANSFORMATION; CHRONIC MYELOID LEUKEMIA; GENE STRUCTURE; HUMAN; HUMAN CELL; MOLECULAR CLONING; MOLECULAR DYNAMICS; ONCOGENE; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SIGNAL TRANSDUCTION;

EID: 0031393127     PISSN: 08939675     EISSN: None     Source Type: Journal    
DOI: 10.1615/CritRevOncog.v8.i4.40     Document Type: Article

References (110)

1. Abercrombie, M. and G. Dunn: Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy. Exp. Cell Res., 92:57-62 (1975).
2. Abercrombie, M., J. Heaysman, and S. Pegrum: The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp. Cell Res., 67:359-367 (1971).
3. Adams, J., H. Houston, J. Allen, T. Lints, and R. Harvey: The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization. Oncogene, 7:611-618 (1992).
4. Avraham, H. and R. Weinberg: Characterization and expression of the human rhoH12 gene product. Mol. Cell. Biol., 9:2058-2066 (1989).
5. Azuma, E. K., S. Kitagawa, A. Yuo, U. Mizoguchi, K. Umezawa, F. Takaku, and M. Saito: Activation of the respitory burst and tyrosine phosphorylation of proteins in human neutrophils - no direct relationship and involvement of protein-kinase C-dependent and C-independent signaling pathways. Biochim. Biophys. Acta, 1179:213-223 (1993).
6. Bedi, A., B. Zehnbauer, J. Barber, S. Sharkis, and R. Jones: Inhibition of apoptosis by BCR-ABL in chronic myeloid leukemia. Blood, 83:2038-2044 (1994).
7. Bennet, P., R. Dixon, and S. Kellie: The phosphotyrosine phosphatase inhibitor vanadyl hydroperoxide induces morphological alterations, cytoskeletal rearrangements, and increased adhesiveness in rat neutrophil leukocytes. J. Cell Sci., 106:891-901 (1993).
8. Bergman, M., V. Joukov, I. Virtanen, and K. Alitalo: 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., 15:15 (1995).
9. Bhatia, R., E. Wayner, P. McGlave, and C. Verfaillie: Interferon-alpha restores normal adhesion of chronic myelogenous leukemia hematopoietic progenitors to bone marrow stroma by correcting impaired beta 1 integrin receptor function. J. Clin. Invest., 94:384-391 (1994).
10. Brickell, P.: The p60c-src family of protein-tyrosine kinases: structure, regulation, and function. Crit. Rev. Oncogen., 3:401-446 (1992).
11. Buck, C. and A. Horwitz: Cell surface receptors for extracellular matrix molecules. Ann. Rev. Cell Biol., 3:179-205 (1987).
12. Burridge, K. and K. Fath: Focal contacts: transmembrane links between the extracellular matrix and the cytoskeleton. Bioessays, 10(4):104-108 (1989).
13. Burridge, K., K. Fath, T. Kelly, G. Nuckolls, and C. Turner: Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Ann. Rev. Cell Biol., 4:487-525 (1988).
14. Burridge, K. and P. Mangeat: An interaction between vinculin and talin. Nature, 308:744-746 (1984).
15. Burridge, K., C. Turner, and L. Romer: Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol., 119:893-904 (1992).
16. Carraway, K. and C. Carraway: Signaling, mitogenesis and the cytoskeleton: where the action is. Bioessays, 17:171-175 (1995).
17. Chiquet-Ehrismann, R.: Tenascin and other adhesion-modulating proteins in cancer. Sem. Cancer Biol., 4: 301-310 (1993).
18. Chissoe, S., A. Bodenteich, Y. Wang, Y. Wang, D. Burian, S. Clifton, J. Crabtree, A. Freeman, K. Iyer, L. Jian et al.: Sequence and analysis of the human ABL gene, the BCR gene, and regions involved in the Philadelphia chromosomal translocation. Genomics, 27:67-82 (1995).
19. Courtneidge, S., A. Levinson, and J. Bishop: The protein encoded by the transforming gene of avian sarcoma virus (pp60src) and a homologous protein in normal cells (pp60 proto-src) are associated with the plasma membrane. Proc. Natl. Acad. Sci. U.S.A., 77:3783-3787 (1980).
20. Daley, G., J. McLaughlin, O. Witte, and D. Baltimore: The CML-specific P210 bcr/abl protein, unlike v-abl, does not transform NIH/3T3 fibroblasts. Science, 237:532-535 (1987).
21. Davis, S., M. Lu, S. Lo, S. Lin, J. Butler, B. Druker, T. Roberts, Q. An, and L. Chen: Presence of an SH2 domain in the actin-binding protein tensin. Science, 252:712-715 (1991).
22. Druker, B., K. Okuda, U. Matulonis, R. Salgia, T. Roberts, and J. Griffin: Tyrosine phosphorylation of rasGAP and associated proteins in chronic myelogenous leukemia cell lines. Blood, 79:2215-2220 (1992).
23. Ehrengruber, M., D. Deranleau, and T. Coates: Shape oscillations of human neutrophil leukocytes: characteriza- tion and relationship to cell motility. J. Exp. Biol., 199:741-747 (1996).
24. Eva, A., G. Vecchio, C. Rao, S. Tronick, and S. Aaronson: The predicted DBL oncogene product defines a distinct class of transforming proteins. Proc. Natl. Acad. Sci. U.S.A., 85:2061-2065 (1988).
25. Evans, R., R. Robson, and M. Stromer: Properties of smooth muscle vinculin. J. Biol. Chem., 259:3916-3924 (1984).
26. Fainstein, E., C. Marcelle, A. Rosner, E. Canaani, R. Gale, O. Dreazen, S. Smith, and C. Croce: A new fused transcript in Philadelphia chromosome positive acute lymphocytic leukaemia. Nature, 330:386-388 (1987).
27. Fiedorek, F. J. and E. Kay: Mapping of the focal adhesion kinase (Fadk) gene to mouse chromosome 15 and human chromosome 8. Mam. Genome, 6:123-126 (1995).
28. Fox, J., L. Lipfert, E. Clark, C. Reynolds, C. Austin, and J. Brugge: On the role of the platelet membrane skeleton in mediating signal transduction. Association of GP IIb-IIIa, pp60c-src, pp62c-yes, and the p21ras GTPase-activating protein with the membrane skeleton. J. Biol. Chem., 268:25973-25984 (1993).
29. Furuta, Y., D. Ilic, S. Kanazawa, N. Takeda, T. Yamamoto, and S. Aizawa: Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene, 11:1989-1995 (1995).
30. Gaertner, A. and A. Wegner: Mechanism of the insertion of actin monomers between the barbed ends of actin filaments and barbed end-bound insertin. J. Musc. Res. & Cell Motil., 12:27-36 (1991).
31. Gavazzi, I., M. V. Nermut, and P. C. Marchisio: Ultrastructure and gold-immunolabelling of cell-substratum adhesions (podosomes) in RSV-transformed BHK cells. J. Cell Sci., 94:85-99 (1989).
32. Giancotti, F. and E. Ruoslahti: Elevated levels of the alpha 5 beta 1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell, 60:849-859 (1990).
33. Gilmore, A., P. Jackson, G. Waites, and D. Critchley: Further characterisation of the talin-binding site in the cytoskeletal protein vinculin. J. Cell Sci., 103:719-731 (1992).
34. Glenney, J. and L. Zokas: Novel tyrosine kinase substrates from rous sarcoma virus-transformed cells are present in the membrane skeleton. J. Cell Biol., 108:2401-2408 (1989).
35. Goga, A., J. McLaughlin, D. Afar, D. Saffran, and O. Witte: Alternative signals to RAS for hematopoietic transformation by the BCR-ABL oncogene. Cell, 82:981-988 (1995).
36. Hanks, S.K., M. B. Calalb, M. C. Harper, and S. K. Patel: Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. U.S.A., 89:8487-8491 (1992).
37. Hanks, S. K. and T. R. Polte: Signaling through focal adhesion kinase. Bioessays, 19:137-145 (1997).
38. Hibi, K., K. Yamakawa, R. Ueda, Y. Horio, Y. Murata, M. Tamari, K. Uchida, T. Takahashi, Y. Nakamura, and T. Takahashi: Aberrant upregulation of a novel integrin alpha subunit gene at 3p21.3 in small cell lung cancer. Oncogene, 9:611-619 (1994).
39. Hildebrand, J., M. Schaller, and J. Parsons: Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol. Biol. Cell, 6:637-647 (1995).
40. Holme, T., S. Kellie, J. Wyke, and N. Crawford: Effect of transformation by Rous sarcoma virus on the character and distribution of actin in Rat-1 fibroblasts: a biochemical and microscopical study. Brit. J. Cancer, 53:53 (1986).
41. Iba, H., F. Cross, E. Garber, and H. Hanafusa: Low level of cellular protein phosphorylation by nontransforming over-produced p60c-src. Mol. Cell. Biol., 5:1058-1066 (1985).
42. Ilic, D., Y. Furuta, S. Kanazawa, N. Takeda, K. Sobue, N. Nakatsuji, S. Nomura, J. Fujimoto, M. Okada, and T. Yamamoto: Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature, 377:539-544 (1995).
43. Ilic, D., S. Kanazawa, Y. Furuta, T. Yamamoto, and S. Aizawa: Impairment of mobility in endodermal cells by FAK deficiency. Exper. Cell Res., 222:298-303 (1996).
44. Inoue, H., N. Tavoloni, and H. Hanafusa: Suppression of v-Src transformation in primary rat embryo fibroblasts. Oncogene, 11:231-238 (1995).
45. Ito, S., D. Werth, N. Richert, and I. Pastan: Vinculin phosphorylation by the src kinase. Interaction of vinculin with phospholipid vesicles. J. Biol. Chem., 258:14626-4631 (1983).
46. Jankowski, S. A. and D. L. Gumucio: Genes for tensin, villin and desmin are linked on mouse chromosome 1. Mam. Genome, 6:744-745 (1995).
47. Johnson, R. and S. Craig: F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature, 373:261-264 (1995).
48. Kefalas, P., T. Brown, and P. Brickell: Signalling by the p60c-src family of protein-tyrosine kinases. Int. J. Biochem. & Cell Biol., 27:551-563 (1995).
49. Kornberg, L., H. Earp, J. Parsons, M. Schaller, and R. Juliano: Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem., 267:23439-23442 (1992).
50. Lewis, J. and M. Schwartz: Mapping in vivo associations of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants. Mol. Biol. Cell, 6:151-160 (1995).
51. Lo, S., Q. An, S. Bao, W. Wong, Y. Liu, P. Janmey, J. Hartwig, and L. Chen: Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence, expression, and characterization. J. Biol. Chem., 269:22310-22319 (1994a).
52. Lo, S. and L. Chen: Focal adhesion as a signal transduction organelle. Cancer Met. Rev., 13:9-24 (1994).
53. Lo, S., P. Janmey, J. Hartwig, and L. Chen: Interactions of tensin with actin and identification of its three distinct actin-binding domains. J. Cell Biol., 125:1067-1075 (1994b).
54. Lo, S., Q. Yu, L. Degenstein, L. Chen, and E. Fuchs: Progressive kidney degeneration in mice lacking tensin. J. Cell Biol., 136:1349-1361 (1997).
55. Lugo, T., A. Pendergast, A. Muller, and O. Witte: Tyrosine kinase activity and transformation potency of bcr/abl oncogene products. Science, 247:1079 (1990).
56. Marchisio, P., O. Capasso, L. Nitsch, R. Cancedda, and E. Gionti: Cytoskeleton and adhesion patterns of cultured chick embryo chondrocytes during cell spreading and Rous sarcoma virus transformation. Exp. Cell Res., 151:332-343 (1984).
57. Marchisio, P. C., D. Cirillo, A. Teti, A. Zambonin-Zallone, and G. Tarone: Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dot-like organization of cytoskeletal proteins involved in microfilament-membrane interactions. Exp. Cell Res., 169:202-214 (1987).
58. Matulonis, U., R. Salgia, K. Okuda, B. Druker, and J. Griffin: Interleukin-3 and p210 BCR/ABL activate both unique and overlapping pathways of signal transduction in a factor-dependent myeloid cell line. Exp. Hematol., 21:1460-1466 (1993).
59. Mazaki, Y., S. Hashimoto, and H. Sabe: Monocyte cells and cancer cells express novel paxillin isoforms with different binding properties to focal adhesion proteins. J. Biol. Chem., 272:7437-7444 (1997).
60. McCarthy, J., A. Skubitz, J. Iida, D. Mooradian, M. Wilke, and L. Furcht: Tumor cell adhesive mechanisms and their relationship to metastasis. Sem. Cancer Biol., 2:155-167 (1991).
61. McGregor, A., A. Blanchard, A. Rowe, and D. Critchley: Identification of the vinculin-binding site in the cytoskeletal protein alpha-actinin. Biochem. J., 301:225-233 (1994).
62. McWhirter, J. and J. Wang: Activation of tyrosine kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins. Mol. Cell Biol., 11:1553-1565 (1991).
63. Miki, T., C. Smith, J. Long, A. Eva, and T. Fleming: Oncogene ect2 is related to regulators of small GTP-binding proteins. Nature, 362:462-465 (1993).
64. Mitchison, T. and L. Cramer: Actin-based cell motility and locomotion. Cell, 84:371-379 (1996).
65. Miyamoto, S., S. Akiyama, and K. Yamada: Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science, 267:883-885 (1995).
66. Mohr, C., G. Koch, I. Just, and K. Aktories: ADP-ribosylation by Clostridium botulinum C3 exoenzyme increases steady-state GTPase activities of recombinant rhoA and rhoB proteins. FEBS Lett., 297:95-99 (1992).
67. Naccache, P., C. Gilbert, A. Caon, M. Gaudry, C. Huang, V. Bonak, K. Umezawa, and S. McColl: Selective inhibition of human neutrophil functional responsiveness by erbstatin, an inhibitor of tyrosine protein kinase. Blood, 76:2098-2104 (1990).
68. Nada, S., M. Okada, S. Aizawa, and H. Nakagawa: Identification of major tyrosine-phosphorylated proteins in Csk-deficient cells. Oncogene, 9:3571-3578 (1994).
69. Nermut, M., P. Eason, E. Hirst, and S. Kellie: Cell/substratum adhesions in RSV-transformed rat fibroblasts. Exp. Cell Res., 193:382-397 (1991).
70. O'Toole, T., Y. Katagiri, R. Faull, K. Peter, R. Tamura, V. Quaranta, J. Loftus, S. Shattil, and M. Ginsberg: Integrin cytoplasmic domains mediate inside-out signal transduction. J. Cell Biol., 124:1047-1059 (1994).
71. Ohsato, Y., S. Nada, M. Okada, and H. Nakagawa: Mitotic activation of c-Src is suppressed by Csk. Jpn. J. Cancer Res., 85:1023-1028 (1994).
72. Oliver, T., J. Lee, and K. Jacobson: Forces exerted by locomoting cells. Semin. Cell Biol, 5:139-147 (1994).
73. Parker, R., H. Varmus, and J. Bishop: Expression of v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src. Cell, 37:131-139 (1984).
74. Perona, R., P. Esteve, B. Jimenez, R. P. Ballestero, S. Ramon y Cajal, and J. C. Lacal: Tumorigenic activity of rho genes from Aplysia californica. Oncogene, 8:1285-1292 (1993).
75. Price, G., P. Jones, M. Davison, B. Patel, R. Bendori,: B. Geiger, and D. Critchley: Primary sequence and domain structure of chicken vinculin. Biochem. J., 259:453-461 (1989).
76. Price, G., P. Jones, M. Davison, B. Patel, I. Eperon, and D. Critchley: Isolation and characterization of a vinculin cDNA from chick-embryo fibroblasts. Biochem. J., 245:595-603 (1987).
77. Qian, F., D. Vaux, and I. Weissman: Expression of the integrin alpha 4 beta 1 on melanoma cells can inhibit the invasive stage of metastasis formation. Cell, 77:335-347 (1994).
78. Renshaw, M., J. McWhirter, and J. Wang: The human leukemia oncogene bcr-abl abrogates the anchorage requirement but not the growth factor requirement for proliferation. Mol. Cell. Biol., 15:1286-1293 (1995).
79. Richardson, A. and T. Parsons: A mechanism for regulation of the adhesion-associated protein tyrosine kinase pp125FAK. Nature, 380:538-540 (1996).
80. Rohrschneider, L.: Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc. Natl. Acad. Sci. U.S.A., 77:3514-3518 (1980).
81. Ron, D., S. Tronick, S. Aaronson, and A. Eva: Molecular cloning and characterization of the human dbl protooncogene: evidence that its overexpression is sufficient to transform NIH/3T3 cells. EMBO J., 7:2465-2473 (1988).
82. Ruhnau, K., A. Gaertner, and A. Wegner: Kinetic evidence for insertion of actin monomers between the barbed ends of actin filaments and barbed end-bound insertin, a protein purified from smooth muscle. J. Mol. Biol., 210:141-148 (1989).
83. Sabe, H., A. Hata, M. Okada, H. Nakagawa, and H. Hanafusa: Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. Proc. Natl. Acad. Sci. U.S.A., 91:3984-3988 (1994).
84. Sager, R., A. Anisowicz, M. Neveu, P. Liang, and G. Sotiropoulou: Identification by differential display of alpha 6 integrin as a candidate tumor suppressor gene. FASEB J., 7:964-970 (1993).
85. Salgia, R., J. Li, S. Lo, B. Brunkhorst, G. Kansas, E. Sobhany, Y. Sun, E. Pisick, M. Hallek, T. Ernst et al: Molecular cloning of human paxillin, a focal adhesion protein phosphorylated by p210BCR/ABL. J. Biol. Chem., 270:5039-5047 (1995).
86. Salgia, R., J.-L. Li, D. Ewaniuk, W. Pear, E. Pisick, S. Burky, T. Ernst, M. Sattler, L. Chen, and J. Griffin: BCR/ABL induces multiple abnormalities of cytoskeletal function. J. Clin. Invest, 100:46-57 (1997).
87. Salgia, R., E. Pisick, M. Sattler, J. L. Li, N. Uemura, W. K. Wong, S. A. Burky, H. Hirai, L. B. Chen, and J. D. Griffin: p130CAS forms a signaling complex with the adapter protein CRKL in hematopoietic cells transformed by the BCR/ABL oncogene. J. Biol. Chem., 271:25198-25203 (1996).
88. Sattler, M. and R. Salgia: Activation of hematopoietic growth factor signal transduction pathways by the human oncogene BCR/ABL. Cytokine & Growth Factor Rev., 8:63-79 (1997).
89. Schaller, M. and J. Parsons: Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol., 6:705-710 (1994).
90. Sefton, B., T. Hunter, E. Ball, and S. Singer: Vinculin: a cytoskeletal target of the transforming protein of Rous sarcoma virus. Cell, 24:165-174 (1981).
91. Serra-Pages, C., N. Kedersha, L. Fazikas, Q. Medley, A. Debant, and M. Streuli: The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions. EMBO J., 14:2827-2838 (1995).
92. Skorski, T., M. Nieborowskaskorska, P. Wlodarski, M. Wasik, R. Trotta, P. Kanakaraj, P. Salomoni, M. Antonyak, R. Martinez, M. Majewski, A. Wong, B. Perussia, and B. Calabretta: The SH3 domain contributes to BCR/ABL-dependent leukemogenesis in vivo -role in adhesion, invasion, and homing. Blood, 91:406-418 (1998).
93. Small, J.: The actin cytoskeleton. Electron Microsc. Rev., 1:155-174 (1988).
94. Sobue, K., K. Kanda, I. Miyamoto, K. Iida, I. Yahara, R. Hirai, and A. Hiragun: Comparison of the regional distribution of calspectin (nonerythroid spectrin or fodrin), alpha-actinin, vinculin nonerythroid protein 4.1, and calpactin in normal and avian sarcoma virus- or Rous sarcoma virus-induced transformed cells. Exp. Cell Res., 181:256-262 (1989).
95. Stallmach, A., B. von Lampe, H. Orzechowski, H. Matthes, and E. Riecken: Increased fibronectin-receptor expression in colon carcinoma-derived HT 29 cells decreases tumorigenicity in nude mice. Gastroenterology, 106:19-27 (1994).
96. Stetler-Stevenson, W., S. Aznavoorian, and L. Liotta: Tumor cell interactions with the extracellular matrix during invasion and metastasis. Ann. Rev. Cell Biol., 9:541-573 (1993).
97. Stossel, T.: The machinery of blood cell movements. Blood, 84:367-379 (1994).
98. Stossel, T.: On the crawling of animal cells. Science, 260:1086-1094 (1993).
99. Superti-Furga, G. and S. Courtneidge: Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays, 17:321-330 (1995).
100. Swanstrom, R., R. Parker, H. Varmus, and J. Bishop: Transduction of a cellular oncogene: the genesis of Rous sarcoma virus. Proc. Natl. Acad. Sci. U.S.A., 80:2519-2523 (1983).
101. Tarone, G., D. Cirillo, F. Giancotti, P. Comoglio, and P. Marchisio: Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res., 159:141-157 (1985).
102. Thomas, S., P. Soriano, and A. Imamoto: Specific and redundant roles of Src and Fyn in organizing the cytoskeleton. Nature, 376:376 (1995).
103. Trouliaris, S., U. Smola, J. Chang, S. Parsons, H. Niemann, and T. Tamura: Tyrosine 807 of the v-Fms oncogene product controls cell morphology and association with p120RasGAP. J. Virol., 69:6010-6020 (1995).
104. Turner, C. E.: Paxillin: a cytoskeletal target for tyrosine kinases. Bioessays, 16:47-52 (1994).
105. Van Etten, R., P. Jackson, D. Baltimore, M. Sanders, P. Matsudaira, and P. Janmey: The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity. J. Cell Biol., 124:325-340 (1994).
106. Verfaillie, C., J. McCarthy, and P. McGlave: Mechanisms underlying abnormal trafficking of malignant progenitors in chronic myelogenous leukemia. Decreased adhesion to stroma and fibronectin but increased adhesion to the basement membrane components laminin and collagen type IV. J. Clin. Invest., 90:1232-1241 (1992).
107. Wilkins, J. and S. Lin: A re-examination of the interaction of vinculin with actin. J. Cell Biol., 102:1085-1092 (1986).
108. Wymann, M., P. Kernen, D. Deranleau, and M. Baggiolini: Respitory burst oscillations in human neutrophils and their correlation with fluctuations in apparent cell shape. J. Biol. Chem., 264:15829-15834 (1989).
109. Yamamoto., M., N. Morii, K. Ikai, and S. Imamura: Effect of botuinum C3 exoenzyme on cell growth and cytoskeleton organization in transformed human epidermal cells in culture: a possible role for rho protein in epidermal cells. J. Dermatol. Sci., 8:103-109 (1994).
110. Zheng, Y., M. Olson, A. Hall, R. Cerione, and D. Toksoz: Direct involvement of the small GTP-binding protein Rho in lbc oncogene function. J. Biol. Chem., 270:9031-9034 (1995).