Arf-like GTPases: not so Arf-like after all

被引：99

作者：

Burd, CG ^{[1
]}

Strochlic, TI ^{[1
]}

Setty, SRG ^{[1
]}

机构：

[1] Univ Penn, Sch Med, Dept Cell & Dev Biol, Philadelphia, PA 19104 USA

来源：

TRENDS IN CELL BIOLOGY | 2004年 / 14卷 / 12期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1016/j.tcb.2004.10.004

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

ADP-ribosylation factor (Arf) GTP-binding proteins are among the best-characterized members of the Ras superfamily of GTPases, with well-established functions in membrane-trafficking pathways. A recent watershed of genomic and structural information has identified a family of conserved related proteins: the Arf-like (Arl) GTPases. The best-characterized Arl protein, Arl2, regulates the folding of 0 tubulin, and recent data suggest that Arl1 and Arf-related protein 1 (ARFRP1) are localized to the trans-Golgi network (TGN), where they function, in part, to regulate the tethering of endosome-derived transport vesicles. Other Arl proteins are localized to the cytosol, nucleus, cytoskeleton and mitochondria, which indicates that Arl proteins have diverse roles that are distinct from the known functions of traditional Arf GTPases.

引用

页码：687 / 694

页数：8

共 67 条

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