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ARF6

From Wikipedia, the free encyclopedia

ARF6
Available structures
PDBOrtholog search:PDBeRCSB
Identifiers
AliasesARF6,ADP-ribosylation factor 6, ADP ribosylation factor 6
External IDsOMIM:600464;MGI:99435;HomoloGene:1256;GeneCards:ARF6;OMA:ARF6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001663

NM_007481

RefSeq (protein)

NP_001654

NP_031507

Location (UCSC)Chr 14: 49.89 – 49.9 MbChr 12: 69.42 – 69.42 Mb
PubMedsearch[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

ADP-ribosylation factor 6(ARF6) is a member of theADP ribosylation factorfamilyofGTP-binding proteins.ARF6 has a variety of cellular functions that are frequently involved in trafficking ofbiological membranesandtransmembrane proteincargo. ARF6 has specifically been implicated inendocytosisofplasma membraneproteins and also, to a lesser extent, plasma membrane protein recycling.

Function

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This gene encodes a member of the human ARF gene family, which is part of theRas 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. Apseudogeneof this gene is located on chromosome 7.[5]

ARF6 can interact with βarrestinuponreceptoractivation.

Interactions

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ARF6 has been shown tointeractwith:

References

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  1. ^abcGRCh38: Ensembl release 89: ENSG00000165527Ensembl,May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000044147Ensembl,May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^"Entrez Gene: ARF6 ADP-ribosylation factor 6".
  6. ^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.PMID11533043.
  7. ^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.PMC1170175.PMID9312003.
  8. ^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.PMID11478794.
  9. ^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.PMID12799371.
  10. ^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.PMC2173613.PMID14662749.
  11. ^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.PMC1538863.PMID16845013.Archived fromthe originalon 2010-04-09.
  12. ^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.PMC3535434.PMID23223291.

Further reading

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