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Vol. 12, No. 21, pp. 3331-3336, November 1, 1998
1 Department of Pathology, National Institute of
Infectious Diseases, Toyama, Shinjuku-ku, Tokyo 162-8640, Japan;
2 First Department of Pathology, Hamamatsu University
School of Medicine, Hamamatsu, Shizuoka 431-3192, Japan;
3 Department of Pathology, Research Institute, International
Medical Center of Japan, Toyama, Shinjuku-ku, Tokyo 162-8655, Japan
DOCK180 is involved in integrin signaling through
CrkII-p130Cas 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 p130Cas 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.
[Key Words: DOCK180; Crk; Rac; mbc; ced-5; guanine nucleotide exchange factor]
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