Journal article
Arf-like GTPases: not so Arf-like after all
Trends in cell biology, v 14(12), pp 687-694
Dec 2004
PMID: 15564045
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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 beta 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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Details
- Title
- Arf-like GTPases: not so Arf-like after all
- Creators
- Christopher G Burd - University of PennsylvaniaTodd I Strochlic - University of PennsylvaniaSubba R Gangi Setty - University of Pennsylvania
- Publication Details
- Trends in cell biology, v 14(12), pp 687-694
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000226018000006
- Scopus ID
- 2-s2.0-9644259237
- Other Identifier
- 991020837745304721
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- Web of Science research areas
- Cell Biology