IPR045872
ADP-ribosylation factor 1-5
InterPro entry
Short name | Arf1-5-like |
Overlapping homologous superfamilies | |
family relationships |
Description
Arf GTPases are involved in the formation of coated carrier vesicles by recruiting coat proteins. This entry includes Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned
[3].
Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins
[1]. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor
[5]. Arf4 has also been shown to recognise the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialised post-Golgi rhodopsin transport carriers (RTCs)
[2]. There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs)
[4].
References
1.Multiple activities for Arf1 at the Golgi complex. Donaldson JG, Honda A, Weigert R. Biochim Biophys Acta 1744, 364-73, (2005). PMID: 15979507
2.Rhodopsin C terminus, the site of mutations causing retinal disease, regulates trafficking by binding to ADP-ribosylation factor 4 (ARF4). Deretic D, Williams AH, Ransom N, Morel V, Hargrave PA, Arendt A. Proc Natl Acad Sci U S A 102, 3301-6, (2005). PMID: 15728366
3.Isoform-selective effects of the depletion of ADP-ribosylation factors 1-5 on membrane traffic. Volpicelli-Daley LA, Li Y, Zhang CJ, Kahn RA. Mol Biol Cell 16, 4495-508, (2005). PMID: 16030262
GO terms
Cross References
ENZYME
Contributing Member Database Entry
- CDD:cd04150