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Evidence That DOCK180 Up-regulates Signals from the CrkII-p130Cas Complex

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Kiyokawa, Etsuko, Hashimoto, Yuko, Kurata, Takeshi, Sugimura, Haruhiko, Matsuda, Michiyuki·1998·Journal of Biological Chemistry

Abstract

DOCK180 is one of the two principal proteins bound to the SH3 domain of the adaptor protein CrkII. Here, we have studied the involvement of DOCK180 in integrin signaling. DOCK180 was neither phosphorylated nor bound to CrkII in quiescent NIH 3T3 cells and 3Y1 cells. We found that DOCK180 was phosphorylated and bound to CrkII in NIH 3T3 cells stimulated with integrin and also in 3Y1 cells transformed by v-src or v-crk. The binding of DOCK180 to CrkII correlated with the binding of CrkII to p130(Cas), which is a major CrkII SH2 domain-binding protein at focal adhesions. In a reconstitution experiment, expression of DOCK180 induced hyperphosphorylation of p130(Cas) and a concomitant increase in the amount of CrkII bound to p130(Cas). Similarly, binding of DOCK180 to CrkII was also enhanced by the coexpression of p130(Cas). Finally, we found that coexpression of p130(Cas) and CrkII with DOCK180 induced local membrane spreading and accumulation of DOCK180-CrkII-p130(Cas) complexes at focal adhesions. These findings suggest that DOCK180 positively regulates signaling from integrins to CrkII-p130(Cas) complexes at focal adhesions.

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Metadata

Authors
Kiyokawa, E., Hashimoto, Y., Kurata, T., Sugimura, H., & Matsuda, M.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-09
Volume
273
Issue
38
Pages
24479-24484
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2034752841
Cited by
208
References
1
FWCI
6.75
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Evidence That DOCK180 Up-regulates Signals from the CrkII-p130Cas Complex. https://app.cochat.ai/papers/10.1074/jbc.273.38.24479
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Kiyokawa, E., Hashimoto, Y., Kurata, T., Sugimura, H., & Matsuda, M. (1998). Evidence That DOCK180 Up-regulates Signals from the CrkII-p130Cas Complex. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.38.24479

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