Article
Regulation of ASAP1 by phospholipids is dependent on the interface between the PH and Arf GAP domains.
Cellular signalling - 1 Oct 2005
Che Magnus M, Boja Emily S, Yoon Hye-Young, Gruschus James, Jaffe Howard, Stauffer Stacey, Schuck Peter, Fales Henry M, Randazzo Paul A
Abstract excerpt
ASAP1 is an Arf GAP with a PH domain immediately N-terminal to the catalytic Arf GAP domain. PH domains are thought to regulate enzymes by binding to specific phosphoinositide lipids in membranes, thereby recruiting the enzyme to a site of action. Here, we have examined the functional relationship between the PH and Arf GAP domains. We found that GAP activity requires the cognate PH domain of ASAP1, leading us to...
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