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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Conference Article|
August 01 2005
The Arf-like GTPase Arl1 and its role in membrane traffic
S. Munro
S. Munro
1
1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, U.K.
1email sean@mrc-lmb.cam.ac.uk
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Publisher: Portland Press Ltd
Received:
April 20 2005
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2005 The Biochemical Society
2005
Biochem Soc Trans (2005) 33 (4): 601–605.
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Received:
April 20 2005
Citation
S. Munro; The Arf-like GTPase Arl1 and its role in membrane traffic. Biochem Soc Trans 1 August 2005; 33 (4): 601–605. doi: https://doi.org/10.1042/BST0330601
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