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Papers In Press, published online ahead of print April 10, 2002
Pathology, Brigham and Women's Hospital, Boston, Massachusetts 02115
Corresponding Author: dsacks{at}rics.bwh.harvard.edu
The Ras-GAP related protein IQGAP1 binds several proteins, including actin, calmodulin, E-cadherin and the Rho family GTPase Cdc42. To gain insight into its in vivo function, IQGAP1 was overexpressed in mammalian cells. Transfection of IQGAP1 significantly increased the levels of active, GTP-bound Cdc42, resulting in the formation of peripheral actin microspikes. By contrast, transfection of an IQGAP1 mutant lacking part of the GAP-related domain (IQGAP1
J. Biol. Chem, 10.1074/jbc.M111165200
Submitted on November 21, 2001
Revised on April 10, 2002
Accepted on April 9, 2002
IQGAP1 is a component of Cdc42 signaling to the cytoskeleton
GRD) substantially decreased the amount of GTP-bound Cdc42 in cell lysates. Consistent with these findings, IQGAP1GRD blocked Cdc42 function in cells which stably overexpress constitutively active Cdc42 and abrogated the effect of bradykinin on Cdc42. In cells transfected with IQGAP1GRD, bradykinin was unable to activate Cdc42, translocate Cdc42 to the membrane fraction or induce filopodia production. IQGAP1GRD transfection altered cellular morphology, producing small, round cells which closely resemble Cdc42-/- cells. Some insight into the mechanism was provided by in vitro analysis which revealed that IQGAP1GRD increased the intrinsic GTPase activity of Cdc42, thereby increasing the amount of inactive, GDP-bound Cdc42. These data imply that IQGAP1 has a crucial role in transducing Cdc42 signaling to the cytoskeleton.
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