From Wikipedia, the free encyclopedia
Jump to: navigation, search
ADP-ribosylation factor 6
Protein ARF6 PDB 1e0s.png
PDB rendering based on 1e0s.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbol ARF6
External IDs OMIM600464 MGI99435 HomoloGene1256 ChEMBL: 5987 GeneCards: ARF6 Gene
RNA expression pattern
PBB GE ARF6 203311 s at tn.png
PBB GE ARF6 203312 x at tn.png
More reference expression data
Species Human Mouse
Entrez 382 11845
Ensembl ENSG00000165527 ENSMUSG00000044147
UniProt P62330 P62331
RefSeq (mRNA) NM_001663 NM_007481
RefSeq (protein) NP_001654 NP_031507
Location (UCSC) Chr 14:
50.36 – 50.36 Mb
Chr 12:
69.37 – 69.38 Mb
PubMed search [1] [2]

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.


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.[1]

ARF6 can interact with βarrestin upon receptor activation.


Arf6 has been shown to interact with:


  1. ^ "Entrez Gene: ARF6 ADP-ribosylation factor 6". 
  2. ^ Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT et al. (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. 
  3. ^ 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 1170175. PMID 9312003. 
  4. ^ 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. 
  5. ^ 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. 
  6. ^ Prigent M, Dubois T, Raposo G, Derrien V, Tenza D, Rossé C et al. (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 2173613. PMID 14662749. 
  7. ^ 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 1538863. PMID 16845013. 
  8. ^ 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 3535434. PMID 23223291. 

Further reading[edit]

External links[edit]

  • Ikeda S, Ushio-Fukai M, Zuo L, Tojo T, Dikalov S, Patrushev NA et al. (2005). "Novel role of ARF6 in vascular endothelial growth factor-induced signaling and angiogenesis". Circ. Res. 96 (4): 467–75. doi:10.1161/01.RES.0000158286.51045.16. PMID 15692085.