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(Received for publication, June 17, 1996)
,
,
,
and
From the Cdc42 and Rac1 have been implicated in the
regulation of various cell functions such as cell morphology, polarity,
and cell proliferation. We have partially purified a Cdc42- and
Rac1-associated protein with molecular mass of about 170 kDa
(p170) from bovine brain cytosol. This protein interacted with
guanosine 5
Division of Signal Transduction, Nara
Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-01, § Department of Biochemistry, Hiroshima University School of
Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734, ¶ Kazusa DNA
Research Institute, 1532-3 Yanauchino, Kisarazu 292, and 
Central
Laboratories for Key Technology, Kirin Brewery Co. Ltd., 1-13-5 Fukuura, Kanazawa-ku, Yokohama 236, Japan
-(3-O-thio)triphosphate
(GTP
S)·glutathione S-transferase (GST)-Cdc42 and
GTPS·GST-Rac1 but not with the GDP·GST-Cdc42, GDP·GST-Rac1, or
GTPS·GST-RhoA). We identified p170 as an IQGAP, which is
originally identified as a putative Ras GTPase-activating
protein. Recombinant IQGAP specifically interacted with
GTPS·Cdc42 and GTPS·Rac1. The C-terminal fragment
of IQGAP was responsible for their interactions. IQGAP was specifically
immunoprecipitated with dominant-active Cdc42Val12 or
Rac1Val12 from the COS7 cells expressing
Cdc42Val12 or Rac1Val12, respectively.
Immunofluorescence analysis revealed that IQGAP was accumulated at
insulin- or Rac1-induced membrane ruffling areas. This accumulation of
IQGAP was blocked by the microinjection of the dominant-negative
Rac1Asn17 or Cdc42Asn17. Moreover, IQGAP was
accumulated at the cell-cell junction in MDCK cells, where 
-catenin
and ZO-1 were localized. These results suggest that IQGAP is a novel
target molecule for Cdc42 and Rac1.
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