The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
The Small G Proteins of the Arf Family and Their Regulators
Abstract
Small G proteins play a central role in the organization of the secretory and endocytic pathways. The majority of such small G proteins are members of the Rab family, which are anchored to the bilayer by C-terminal prenyl groups. However, the recruitment of some effectors, including vesicle coat proteins, is mediated by a second class of small G proteins that is unique in having an N-terminal amphipathic helix that becomes available for membrane insertion upon GTP binding. Sar1, Arf1, and Arf6 are the best-characterized members of this ADP-ribosylation factor (Arf) family. In addition, all eukaryotes contain additional distantly related G proteins, often called Arf like, or Arls. The complete Arf family in humans has 29 members. The roles of these related G proteins are poorly understood, but recent work has shown that some are involved in membrane traffic or organizing the cytoskeleton. Here we review what is known about all the members of the Arf family, along with the known regulatory molecules that convert them between GDP- and GTP-bound states.
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Cites
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
TreeFam: a curated database of phylogenetic trees of animal gene families
Li, H. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj118 · Cited by 523
Brefeldin A Acts to Stabilize an Abortive ARF–GDP–Sec7 Domain Protein Complex
Peyroche, A., Antonny, B., Robineau, S., Acker, J., Cherfils, J., & Jackson, C. L. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80455-4 · Cited by 453
Cited by
BORC, a Multisubunit Complex that Regulates Lysosome Positioning
Pu, J., Schindler, C., Jia, R., Jarnik, M., Backlund, P., & Bonifacino, J. S. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.02.011 · Cited by 406
Toward a Comprehensive Map of the Effectors of Rab GTPases
Gillingham, A. K., Sinka, R., Torres, I. L., Lilley, K. S., & Munro, S. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.10.007 · Cited by 283
Self-citationArl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo
Ismail, S. A., Chen, Y.-X., Rusinova, A., Chandra, A., Bierbaum, M., Gremer, L., Triola, G., Waldmann, H., Bastiaens, P. I. H., & Wittinghofer, A. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.686 · Cited by 252
Ciliary targeting motif VxPx directs assembly of a trafficking module through Arf4
Mazelova, J., Astuto‐Gribble, L., Inoue, H., Tam, B. M., Schonteich, E., Prekeris, R., Moritz, O. L., Randazzo, P. A., & Deretic, D. (2009) · The EMBO Journal · doi:10.1038/emboj.2008.267 · Cited by 244
Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins
Sinka, R., Gillingham, A. K., Kondylis, V., & Munro, S. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200808018 · Cited by 190
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Metadata
- Authors
- Gillingham, A. K., & Munro, S.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2007-11-01
- Volume
- 23
- Issue
- 1
- Pages
- 579-611
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2127432085
- Cited by
- 591
- References
- 3
- FWCI
- 1.76
- Type
- journal article
- Language
- en
- Open access
- closed
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