Toward a Structural Understanding of Art Family: Effector Specificity

被引：21

作者：

Chavrier, Philippe ^{[1
,2
]}

Menetrey, Julie ^{[3
]}

机构：

[1] Ctr Rech, Inst Curie, F-75248 Paris, France

[2] CNRS, UMR144, F-75248 Paris, France

[3] CNRS, Ctr Rech Gif, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France

来源：

STRUCTURE | 2010年 / 18卷 / 12期

关键词：

GTP-BINDING PROTEINS; ADP-RIBOSYLATION; CHOLERA-TOXIN; MEMBRANE RECRUITMENT; CRYSTAL-STRUCTURE; GOLGI-APPARATUS; SAR PROTEINS; GRIP DOMAINS; RAB GTPASES; PDE-DELTA;

D O I：

10.1016/j.str.2010.11.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Art family proteins are critical regulators of intracellular trafficking and actin cytoskeleton dynamics. To carry out their cellular functions, Arf family proteins interact with various effectors that differ in nature and structure. Understanding how these proteins interact with structurally different partners and are distinguished by specific effectors while being closely related requires a structural characterization and comparison of the various Art family:effector complexes. Recent structural reports of Art and Art proteins in complex with different downstream effectors shed new light on general and specific structural recognition determinants characteristic of Art family proteins.

引用

页码：1552 / 1558

页数：7

共 41 条

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