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Article

Dynamic interaction between Arf GAP and PH domains of ASAP1 in the regulation of GAP activity.

Cellular signalling - 1 Nov 2008

Luo Ruibai, Miller Jenkins Lisa M, Randazzo Paul A, Gruschus James

Abstract excerpt

ASAP family Arf GAPs induce the hydrolysis of GTP bound to the Ras superfamily protein Arf1, regulate cell adhesion and migration and have been implicated in carcinogenesis. The ASAP proteins have a core catalytic domain of PH, Arf GAP and Ank repeat domains. The PH domain is necessary for both biological and catalytic functions of ASAP1 and has been proposed to be integrally folded with the Arf GAP domain....

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Identifiers

PMID: 18675341
DOI: 10.1016/j.cellsig.2008.07.007
PMCID: PMC2574850

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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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