Assays and properties of the Arf GAPs AGAP1, ASAP1, and Arf GAP1

被引：17

作者：

Che, MM ^{[1
]}

Nie, ZZ ^{[1
]}

Randazzo, PA ^{[1
]}

机构：

[1] NCI, Cellular Oncol Lab, Canc Res Ctr, NIH, Bethesda, MD 20892 USA

来源：

GTPASES REGULATING MEMBRANE DYNAMICS | 2005年 / 404卷

关键词：

D O I：

10.1016/S0076-6879(05)04015-2

中图分类号：

Q5 [生物化学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

ADP-ribosylation factors (Arfs) are Ras-like GTP-binding proteins that regulate membrane traffic and actin remodeling. Arf function requires GTP hydrolysis but Arf lacks GTPase activity; consequently, Arf function is dependent on Arf GTPase-activating proteins (GAPS). The Arf GAPS are a structurally diverse group of at least 16 proteins. Several Arf GAPS use a single Arf isoform. However, due to structural differences, the conditions supporting productive interactions between Arf and different Arf GAPS vary. Here, we describe preparation and basic properties of three Arf GAPS. We use these proteins to illustrate assays for Arf GAP activity. Conditions that optimize activity for each GAP are discussed. These methods can be used for the further characterization of Arf-Arf GAP interaction that is necessary for understanding the function of Arf in cellular physiology.

引用

页码：147 / 163

页数：17

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