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J Biol Chem, Vol. 274, Issue 37, 26044-26050, September 10, 1999
-Catenin
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From the IQGAP1, a target of Cdc42 and Rac1 small GTPases,
directly interacts with Division of Signal Transduction, Department of Virology II, Institute for
Virus Research,
-catenin and negatively regulates
E-cadherin-mediated cell-cell adhesion by dissociating 
-catenin from
the cadherin-catenin complex in vivo (Kuroda, S., Fukata,
M., Nakagawa, M., Fujii, K., Nakamura, T., Ookubo, T., Izawa, I.,
Nagase, T., Nomura, N., Tani, H., Shoji, I., Matsuura, Y., Yonehara,
S., and Kaibuchi, K. (1998) Science 281, 832-835). Here we
investigated how Cdc42 and Rac1 regulate the IQGAP1 function. IQGAP1
interacted with the amino-terminal region (amino acids 1-183) of
-catenin, which contains the -catenin-binding domain. IQGAP1
dissociated -catenin from the -catenin--catenin complex in a
dose-dependent manner in vitro. Guanosine
5'-(3-O-thio)triphosphate (GTP
S)·glutathione S-transferase (GST)-Cdc42 and GTPS·GST-Rac1 inhibited
the binding of IQGAP1 to -catenin in a dose-dependent
manner in vitro, whereas neither GDP·GST-Cdc42,
GDP·GST-Rac1, nor GTPS·GST-RhoA did. The coexpression of
dominant active Cdc42 with IQGAP1 suppressed the dissociation of
-catenin from the cadherin-catenin complex induced by the
overexpression of IQGAP1 in L cells expressing E-cadherin (EL cells).
Consistent with this, the overexpression of either dominant negative
Cdc42 or Rac1 resulted in the reduction of E-cadherin-mediated cell
adhesive activity in EL cells. These results indicate that Cdc42 and
Rac1 negatively regulate the IQGAP1 function by inhibiting the
interaction of IQGAP1 with -catenin, leading to stabilization of the
cadherin-catenin complex.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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