Activation of Rac1 by a Crk SH3-binding protein, DOCK180
Etsuko Kiyokawa(Hamamatsu University School of Medicine), Yuko Hashimoto(Hamamatsu University School of Medicine), Shin Kobayashi(Hamamatsu University School of Medicine), Haruhiko Sugimura(Hamamatsu University School of Medicine), Takeshi Kurata(Hamamatsu University School of Medicine), Michiyuki Matsuda(Hamamatsu University School of Medicine)
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Abstract
DOCK180 is involved in integrin signaling through CrkII-p130(Cas) complexes. We have studied the involvement of DOCK180 in Rac1 signaling cascades. DOCK180 activated JNK in a manner dependent on Rac1, Cdc42Hs, and SEK, and overexpression of DOCK180 increased the amount of GTP-bound Rac1 in 293T cells. Coexpression of CrkII and p130(Cas) enhanced this DOCK180-dependent activation of Rac1. Furthermore, we observed direct binding of DOCK180 to Rac1, but not to RhoA or Cdc42Hs. Dominant-negative Rac1 suppressed DOCK180-induced membrane spreading. These results strongly suggest that DOCK180 is a novel activator of Rac1 and involved in integrin signaling.
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