Abstract
Small GTP-binding proteins of the Rab and Arf (ADP-ribosylation factor) families play a central role in the membrane trafficking pathways of eukaryotic cells. The prototypical members of the Arf family are Arf1–Arf6 and Sar1, which have well-characterized roles in membrane traffic or cytoskeletal reorganization. However, eukaryotic genomes encode additional proteins, which share the characteristic structural features of the Arf family, but the role of these ‘Arf-like’ (Arl) proteins is less well understood. This review discusses Arl1, a GTPase that is widely conserved in evolution, and which is localized to the Golgi in all species so far examined. The best-characterized effectors of Arl1 are coiled-coil proteins which share a C-terminal GRIP domain, but other apparent effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps fifty-three) vesicle-tethering complex and Arfaptin 2. As least some of these proteins are believed to have a role in membrane traffic. Genetic analysis in a number of species has shown that Arl1 is not essential for exocytosis, but rather suggest that it is required for traffic from endosomes to the Golgi.
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Dates
Type | When |
---|---|
Created | 20 years ago (Aug. 3, 2005, 8:51 a.m.) |
Deposited | 3 years, 9 months ago (Nov. 17, 2021, 4:57 p.m.) |
Indexed | 5 months, 2 weeks ago (March 19, 2025, 9:58 a.m.) |
Issued | 20 years, 1 month ago (Aug. 1, 2005) |
Published | 20 years, 1 month ago (Aug. 1, 2005) |
Published Online | 20 years, 1 month ago (Aug. 1, 2005) |
Published Print | 20 years, 1 month ago (Aug. 1, 2005) |
@article{Munro_2005, title={The Arf-like GTPase Arl1 and its role in membrane traffic}, volume={33}, ISSN={1470-8752}, url={http://dx.doi.org/10.1042/bst0330601}, DOI={10.1042/bst0330601}, number={4}, journal={Biochemical Society Transactions}, publisher={Portland Press Ltd.}, author={Munro, S.}, year={2005}, month=aug, pages={601–605} }