IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross- links microfilaments

Anne Marie Bashour, Aaron T. Fullerton, Matthew J. Hart, George S. Bloom

Research output: Contribution to journalArticle

199 Scopus citations

Abstract

Activated forms of the GTPases, Rac and Cdc42, are known to stimulate formation of microfilament-rich lamellipodia and filopodia, respectively, but the underlying mechanisms have remained obscure. We now report the purification and characterization of a protein, IQGAP1, which is likely to mediate effects of these GTPases on microfilaments. Native IQGAP1 purified from bovine adrenal comprises two ≃190-kD subunits per molecule plus substoichiometric calmodulin. Purified IQGAP1 bound directly to F-actin and cross-linked the actin filaments into irregular, interconnected bundles that exhibited gel-like properties. Exogenous calmodulin partially inhibited binding of IQGAP1 to F-actin, and was more effective in the absence, than in the presence of calcium. Immunofluorescence microscopy demonstrated cytochalasin D-sensitive colocalization of IQGAP1 with cortical microfilaments. These results, in conjunction with prior evidence that IQGAP1 binds directly to activated Rac and Cdc42, suggest that IQGAP1 serves as a direct molecular link between these GTPases and the actin cytoskeleton, and that the actin-binding activity of IQGAP1 is regulated by calmodulin.

Original languageEnglish (US)
Pages (from-to)1555-1566
Number of pages12
JournalJournal of Cell Biology
Volume137
Issue number7
DOIs
StatePublished - Jun 30 1997
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

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