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Licensed Unlicensed Requires Authentication Published by De Gruyter January 10, 2007

Asef is a Cdc42-specific guanine nucleotide exchange factor

  • Katja Gotthardt and Mohammad Reza Ahmadian
From the journal Biological Chemistry

Abstract

Asef is a member of the Dbl-family of guanine nucleotide exchange factors (GEFs) with a proposed specificity for the small GTPase Rac1. Here we investigated the specificity and regulation of Asef by measuring its GEF activity in vitro and observed hardly any activity towards Rac1, Rac2 and Rac3, or RhoA and TC10. In contrast, various purified Asef protein fragments catalyzed the nucleotide exchange reaction of Cdc42. The Cdc42GEF activity of the Dbl homology (DH) domain of Asef was significantly higher in the presence of the pleckstrin homology (PH) domain. Our data strongly suggest that Asef is a canonical Cdc42GEF, which employs its PH domain to efficiently stabilize its autoinhibited state, but also to facilitate nucleotide exchange activity of the DH domain after its activation by upstream signals.

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Corresponding author

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Published Online: 2007-01-10
Published in Print: 2007-01-01

©2007 by Walter de Gruyter Berlin New York

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