ARF6

ARF6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases ARF6, ADP-ribosylation factor 6
External IDs OMIM: 600464 MGI: 99435 HomoloGene: 1256 GeneCards: ARF6
RNA expression pattern


More reference expression data
Orthologs
Species Human Mouse
Entrez

382

11845

Ensembl

ENSG00000165527

ENSMUSG00000044147

UniProt

P62330

P62331

RefSeq (mRNA)

NM_001663

NM_007481

RefSeq (protein)

NP_001654.1

NP_031507.1

Location (UCSC) Chr 14: 49.89 – 49.9 Mb Chr 12: 69.37 – 69.38 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

ADP-ribosylation factor 6 (ARF6) is a member of the ADP ribosylation factor family of GTP-binding proteins. ARF6 has a variety of cellular functions that are frequently involved in trafficking of biological membranes and transmembrane protein cargo. ARF6 has specifically been implicated in endocytosis of plasma membrane proteins and also, to a lesser extent, plasma membrane protein recycling.

Function

This gene encodes a member of the human ARF gene family, which is part of the RAS superfamily. The ARF genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The product of this gene is localized to the plasma membrane, and regulates vesicular trafficking, remodelling of membrane lipids, and signaling pathways that lead to actin remodeling. A pseudogene of this gene is located on chromosome 7.[3]

ARF6 can interact with βarrestin upon receptor activation.

Interactions

Arf6 has been shown to interact with:

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. "Entrez Gene: ARF6 ADP-ribosylation factor 6".
  4. Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (November 2001). "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45): 42509–13. doi:10.1074/jbc.M108399200. PMID 11533043.
  5. D'Souza-Schorey C, Boshans RL, McDonough M, Stahl PD, Van Aelst L (September 1997). "A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements". EMBO J. 16 (17): 5445–54. doi:10.1093/emboj/16.17.5445. PMC 1170175Freely accessible. PMID 9312003.
  6. Shin OH, Exton JH (August 2001). "Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1". Biochem. Biophys. Res. Commun. 285 (5): 1267–73. doi:10.1006/bbrc.2001.5330. PMID 11478794.
  7. Mitchell R, Robertson DN, Holland PJ, Collins D, Lutz EM, Johnson MS (September 2003). "ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor". J. Biol. Chem. 278 (36): 33818–30. doi:10.1074/jbc.M305825200. PMID 12799371.
  8. Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C, Camonis J, Chavrier P (December 2003). "ARF6 controls post-endocytic recycling through its downstream exocyst complex effector". J. Cell Biol. 163 (5): 1111–21. doi:10.1083/jcb.200305029. PMC 2173613Freely accessible. PMID 14662749.
  9. Prieto C, De Las Rivas J (July 2006). "APID: Agile Protein Interaction DataAnalyzer". Nucleic Acids Res. 34 (Web Server issue): W298–302. doi:10.1093/nar/gkl128. PMC 1538863Freely accessible. PMID 16845013.
  10. Peru y Colón de Portugal RL, Acevedo SF, Rodan AR, Chang LY, Eaton BA, Rothenfluh A (December 2012). "Adult neuronal Arf6 controls ethanol-induced behavior with Arfaptin downstream of Rac1 and RhoGAP18B". J. Neurosci. 32 (49): 17706–13. doi:10.1523/JNEUROSCI.1944-12.2012. PMC 3535434Freely accessible. PMID 23223291.

Further reading

External links

This article is issued from Wikipedia - version of the 6/2/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.