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Gene Review

ARF5  -  ADP-ribosylation factor 5

Homo sapiens

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Disease relevance of ARF5


High impact information on ARF5

  • Hexahistidine-tagged-GBF1 exhibited BFA-resistant guanine nucleotide exchange activity that appears specific towards ARF5 at physiological Mg2+concentration [2].
  • Similar experiments with mutants of ARF5 and ARF6 showed that these other ARF family members had little or no effect on AP-3 [3].
  • ARF 1 accumulated in microsomes plus Golgi and Golgi fractions, whereas ARF 5 seemed to localize more specifically in Golgi; the smaller increment in ARF 3 was distributed more evenly among fractions [4].
  • We further show that Arf1 and Arf5, but not Arf6, are BFA-sensitive, despite their having every BFA-interacting residue in common [5].
  • We describe a related protein, arfophilin-2, that interacts with Arf5 in a nucleotide-dependent manner, but not Arf1, 4, or 6 and also binds Rab11 [6].

Biological context of ARF5

  • With six coding exons and five introns, the genomic structure of ARF5 is unique among the mammalian ARF genes and provides insight about the evolutionary history of this ancient gene family [7].
  • We have mapped ARF5, one of the six known mammalian ARF genes, to a well-defined yeast artificial chromosome contig on human chromosome 7q31 [7].
  • The level of ARF5 gene expression, therefore, is dependent upon Sp1 or an Sp1-like factor but does not rely upon a canonical initiator element for accurate transcription initiation [1].
  • ARF 5 was most similar in deduced amino acid sequence to ARF 4, which also has 180 amino acids [8].

Anatomical context of ARF5

  • Myristoylated ARF5, however, demonstrated a temperature- and GTP-dependent association with Golgi membranes, whereas non-myristoylated ARF did not bind to Golgi under any of the experimental conditions [9].
  • Hybridization of a blot containing 50 human RNAs with an ADP-ribosylation factor 5-specific (ARF5) oligonucleotide probe revealed that the ARF5 gene is expressed in all tissues; however, the level of expression varies significantly with highest levels in pancreas, pituitary gland, and placenta [1].
  • With mammalian poly(A)+ RNA from a variety of tissues and cultured cells, ARF 5 preferentially hybridized with a 1.3-kb mRNA, whereas ARF 6 hybridized with 1.8- and 4.2-kb mRNAs [8].
  • We show that Arf6 has a predominant role in neurite extension compared with Arf1 and Arf5 [10].

Associations of ARF5 with chemical compounds

  • We observe that the NH2 termini of Group II ARFs (ARF4 and ARF5) are efficiently processed by removal of the initiating methionine [11].
  • She developed ARF 5 months following implantation, concurrent with an elevated serum tobramycin concentration of 5.5 microg/mL [12].

Other interactions of ARF5

  • Unexpectedly, PLD2 lacking this region becomes highly responsive to ARF proteins and displays a modest preference for activation by ARF5 [13].
  • The ratios of Bcl-2/GAPDH normalized to calibrator were as follows: LIV 48 +/- 30, CAD-PF 38 +/- 55, and CAD-ARF 5 +/- 7 (p < 0.05) [14].

Analytical, diagnostic and therapeutic context of ARF5

  • Electrophoretic mobility-shift assays demonstrated specific DNA/protein complexes could be formed with oligonucleotides containing each of the GC boxes and these complexes could be effectively competed by oligonucleotides containing either ARF5 Sp1 site or by an oligonucleotide containing a previously characterized Sp1-binding sequence [1].


  1. Transcriptional regulation of the human ADP-ribosylation factor 5 (ARF5) gene. Lebeda, R.A., Johnson, S.K., Haun, R.S. Biochim. Biophys. Acta (1999) [Pubmed]
  2. GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. Claude, A., Zhao, B.P., Kuziemsky, C.E., Dahan, S., Berger, S.J., Yan, J.P., Armold, A.D., Sullivan, E.M., Melançon, P. J. Cell Biol. (1999) [Pubmed]
  3. ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. Ooi, C.E., Dell'Angelica, E.C., Bonifacino, J.S. J. Cell Biol. (1998) [Pubmed]
  4. Differential interaction of ADP-ribosylation factors 1, 3, and 5 with rat brain Golgi membranes. Tsai, S.C., Adamik, R., Haun, R.S., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  5. Dual specificity of the interfacial inhibitor brefeldin a for arf proteins and sec7 domains. Zeeh, J.C., Zeghouf, M., Grauffel, C., Guibert, B., Martin, E., Dejaegere, A., Cherfils, J. J. Biol. Chem. (2006) [Pubmed]
  6. Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout. Hickson, G.R., Matheson, J., Riggs, B., Maier, V.H., Fielding, A.B., Prekeris, R., Sullivan, W., Barr, F.A., Gould, G.W. Mol. Biol. Cell (2003) [Pubmed]
  7. Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene. McGuire, R.E., Daiger, S.P., Green, E.D. Genomics (1997) [Pubmed]
  8. Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells. Tsuchiya, M., Price, S.R., Tsai, S.C., Moss, J., Vaughan, M. J. Biol. Chem. (1991) [Pubmed]
  9. Effect of myristoylation on GTP-dependent binding of ADP-ribosylation factor to Golgi. Haun, R.S., Tsai, S.C., Adamik, R., Moss, J., Vaughan, M. J. Biol. Chem. (1993) [Pubmed]
  10. ADP-ribosylation factor 6 and a functional PIX/p95-APP1 complex are required for Rac1B-mediated neurite outgrowth. Albertinazzi, C., Za, L., Paris, S., de Curtis, I. Mol. Biol. Cell (2003) [Pubmed]
  11. Analysis of recombinant human ADP-ribosylation factors by reversed-phase high-performance liquid chromatography and electrospray mass spectrometry. Berger, S.J., Claude, A.C., Melançon, P. Anal. Biochem. (1998) [Pubmed]
  12. Acute renal failure associated with vancomycin- and tobramycin-laden cement in total hip arthroplasty. Patrick, B.N., Rivey, M.P., Allington, D.R. The Annals of pharmacotherapy. (2006) [Pubmed]
  13. Molecular analysis of mammalian phospholipase D2. Sung, T.C., Altshuller, Y.M., Morris, A.J., Frohman, M.A. J. Biol. Chem. (1999) [Pubmed]
  14. Failure of BCL-2 up-regulation in proximal tubular epithelial cells of donor kidney biopsy specimens is associated with apoptosis and delayed graft function. Schwarz, C., Hauser, P., Steininger, R., Regele, H., Heinze, G., Mayer, G., Oberbauer, R. Lab. Invest. (2002) [Pubmed]
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