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ADP-ribosylation factor 6
PBB Protein ARF6 image.jpg
PDB rendering based on 1e0s.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Symbols ARF6 ;
External IDs Template:OMIM5 Template:MGI HomoloGene1256
RNA expression pattern
PBB GE ARF6 203311 s at tn.png
PBB GE ARF6 203312 x at tn.png
More reference expression data
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

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.


  1. "Entrez Gene: ARF6 ADP-ribosylation factor 6".

Further reading

  • Sabe H (2004). "Requirement for Arf6 in cell adhesion, migration, and cancer cell invasion". J. Biochem. 134 (4): 485–9. PMID 14607973.
  • Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. PMID 15638726.
  • Tsuchiya M, Price SR, Tsai SC; et al. (1991). "Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells". J. Biol. Chem. 266 (5): 2772–7. PMID 1993656.
  • Stearns T, Willingham MC, Botstein D, Kahn RA (1990). "ADP-ribosylation factor is functionally and physically associated with the Golgi complex". Proc. Natl. Acad. Sci. U.S.A. 87 (3): 1238–42. PMID 2105501.
  • D'Souza-Schorey C, Stahl PD (1995). "Myristoylation is required for the intracellular localization and endocytic function of ARF6". Exp. Cell Res. 221 (1): 153–9. doi:10.1006/excr.1995.1362. PMID 7589240.
  • D'Souza-Schorey C, Li G, Colombo MI, Stahl PD (1995). "A regulatory role for ARF6 in receptor-mediated endocytosis". Science. 267 (5201): 1175–8. PMID 7855600.
  • Welsh CF, Moss J, Vaughan M (1995). "ADP-ribosylation factors: a family of approximately 20-kDa guanine nucleotide-binding proteins that activate cholera toxin". Mol. Cell. Biochem. 138 (1–2): 157–66. PMID 7898460.
  • Amor JC, Harrison DH, Kahn RA, Ringe D (1995). "Structure of the human ADP-ribosylation factor 1 complexed with GDP". Nature. 372 (6507): 704–8. doi:10.1038/372704a0. PMID 7990966.
  • Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol". Nature. 364 (6439): 732–4. doi:10.1038/364732a0. PMID 8355790.
  • Helms JB, Palmer DJ, Rothman JE (1993). "Two distinct populations of ARF bound to Golgi membranes". J. Cell Biol. 121 (4): 751–60. PMID 8491770.
  • Cavenagh MM, Whitney JA, Carroll K; et al. (1996). "Intracellular distribution of Arf proteins in mammalian cells. Arf6 is uniquely localized to the plasma membrane". J. Biol. Chem. 271 (36): 21767–74. PMID 8702973.
  • D'Souza-Schorey C, Boshans RL, McDonough M; et al. (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. PMID 9312003.
  • Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6". J. Biol. Chem. 273 (1): 23–7. PMID 9417041.
  • Yang CZ, Heimberg H, D'Souza-Schorey C; et al. (1998). "Subcellular distribution and differential expression of endogenous ADP-ribosylation factor 6 in mammalian cells". J. Biol. Chem. 273 (7): 4006–11. PMID 9461590.
  • Mao M, Fu G, Wu JS; et al. (1998). "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 8175–80. PMID 9653160.
  • Andreev J, Simon JP, Sabatini DD; et al. (1999). "Identification of a new Pyk2 target protein with Arf-GAP activity". Mol. Cell. Biol. 19 (3): 2338–50. PMID 10022920.
  • Radhakrishna H, Al-Awar O, Khachikian Z, Donaldson JG (1999). "ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements". J. Cell. Sci. 112 ( Pt 6): 855–66. PMID 10036235.
  • Kim HS (1999). "Assignment of the human ADP-ribosylation factor 6 (ARF6) gene to chromosome 7q22.1 by radiation hybrid mapping". Cytogenet. Cell Genet. 84 (1–2): 94. PMID 10343114.
  • Langille SE, Patki V, Klarlund JK; et al. (1999). "ADP-ribosylation factor 6 as a target of guanine nucleotide exchange factor GRP1". J. Biol. Chem. 274 (38): 27099–104. PMID 10480924.
  • Honda A, Nogami M, Yokozeki T; et al. (1999). "Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation". Cell. 99 (5): 521–32. PMID 10589680.

External links

  • Ikeda S, Ushio-Fukai M, Zuo L; 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.