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Cell Growth & Differentiation Vol. 13, 131-139, March 2002
© 2002 American Association for Cancer Research

Signaling Adaptor Protein v-Crk Activates Rho and Regulates Cell Motility in 3Y1 Rat Fibroblast Cell Line1

Masumi Tsuda, Shinya Tanaka2, Hirofumi Sawa, Hidesaburo Hanafusa and Kazuo Nagashima

Laboratory of Molecular and Cellular Pathology, Hokkaido University School of Medicine, Sapporo 060-8638 [M. T., S. T., H. S., K. N.]; CREST, Japan Science and Technology Corporation [M. T., S. T., H. S., K. N.]; and Osaka Bioscience Institute, Osaka 565-0874 [H. H.], Japan

The adaptor protein Crk has been reported to associate with focal adhesions and is thought to be involved in integrin-mediated signaling pathway. However, the precise mechanism of Crk-dependent regulation of cytoskeleton still remains under investigation. In this study, we have established a v-Crk-inducible cell line in rat fibroblasts 3Y1 cells and found that v-Crk activated Rho and induced actin stress fiber formation. In addition to the induction of tyrosine-phosphorylation of p130Cas and paxillin, we demonstrated that v-Crk induced threonine-phosphorylated bands sized at 72/78 kDa found specifically in 3Y1 cells. Both of the inhibitors of Rho and Rho-associated kinase, C3 and Y27632, respectively, inhibited these v-Crk-induced biochemical effects. Although v-Crk-induced cells exhibited a decrease of cell motility, integrin stimulation recovered the suppression of motility. Furthermore, v-Crk enhanced motility in chemotactic assay toward fibronectin with additional activation of Rho and the increase of levels of CD44 cleavage. These results suggest that v-Crk activated Rho and induced actin stress fiber formation and CD44 cleavage leading to the regulation of cell motility.




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Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 2002 by the American Association of Cancer Research.