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

ADP核糖基化因子 生物 GTP酶 细胞生物学 GTP结合蛋白调节剂 微管 Ras超家族 细胞骨架 胞浆 内体 高尔基体 GTPase激活蛋白 小型GTPase 转运蛋白 GTP' G蛋白 生物化学 信号转导 细胞内 内质网 细胞
作者
Christopher G. Burd,Todd I. Strochlic,Subba Rao Gangi Setty
出处
期刊:Trends in Cell Biology [Elsevier BV]
卷期号:14 (12): 687-694 被引量:113
标识
DOI:10.1016/j.tcb.2004.10.004
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 β 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. 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 β 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.
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