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Article

A stretch of polybasic residues mediates Cdc42 GTPase-activating protein (CdGAP) binding to phosphatidylinositol 3,4,5-trisphosphate and regulates its GAP activity.

The Journal of biological chemistry - 1 Jun 2012

Karimzadeh Fereshteh, Primeau Martin, Mountassif Driss, Rouiller Isabelle, Lamarche-Vane Nathalie

Abstract excerpt

The Rho family of small GTPases are membrane-associated molecular switches involved in the control of a wide range of cellular activities, including cell migration, adhesion, and proliferation. Cdc42 GTPase-activating protein (CdGAP) is a phosphoprotein showing GAP activity toward Rac1 and Cdc42. CdGAP activity is regulated in an adhesion-dependent manner and more recently, we have identified CdGAP as a novel...

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Identifiers

PMID: 22518840
DOI: 10.1074/jbc.M112.344606
PMCID: PMC3365996

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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