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Gene Review

Arf1  -  ADP-ribosylation factor 1

Mus musculus

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Disease relevance of Arf1


High impact information on Arf1


Biological context of Arf1

  • Instead, termination of Arf1 signals mediated through GGA require that Arf1.GTP dissociates from GGA prior to interaction with GAP and consequent hydrolysis of GTP [5].
  • BACKGROUND: Arf GAPs are multidomain proteins that function in membrane traffic by inactivating the GTP binding protein Arf1 [6].
  • In addition, similar up-regulation of translation was observed when Staufen1 was tethered to the 5' end of mRNAs via other structured RNAs, the highest level of translational increase being obtained with the bona fide Staufen1-binding site of the Arf1 transcript [7].
  • ASAP1 (ADP ribosylation factor [ARF]- GTPase-activating protein [GAP] containing SH3, ANK repeats, and PH domain) is a phospholipid-dependent ARF-GAP that binds to and is phosphorylated by pp60(Src) [8].
  • Similar to ARF GAPs, the GAP domain of ARD1 contains a zinc finger motif and arginine residues that are critical for activity [9].

Anatomical context of Arf1

  • Evidence is provided that 3A inhibits the activation of the GTPase ADP-ribosylation factor 1 (Arf1), which regulates the recruitment of the COP-I coat complex to membranes [10].
  • In the present study, two mutant forms of Sar1 and ARF1 (ADP-ribosylation factor 1) were used to disrupt cargo exit from ER-exit sites and intra-Golgi trafficking in skeletal-muscle fibres respectively [11].
  • Moreover, leakage of endogenous ARF from cells was coincident with loss of GTPgammaS- induced redistribution of paxillin to focal adhesions, and the response was recovered by addition of ARF1 [3].
  • On addition of these truncated fragments to AP-1-depleted adrenal cytosol, both types of core fragments were efficiently recruited onto Golgi membranes in the presence of GTP gamma S. Recruitment of both core fragments was inhibited by the fungal metabolite brefeldin A, indicative of an ARF-dependent process [12].
  • Moreover, we were successful in transfecting a dominant-negative ADP ribosylation factor 1 (ARF1) mutant, i.e., ARF1N126I, in myotubes, thus interfering with endoplasmic reticulum-Golgi traffic, as indicated by alterations of subcellular distribution of GM130, a cis/medial-Golgi marker [13].

Associations of Arf1 with chemical compounds

  • Arf1-dependent PLD1 is localized to oleic acid-induced lipid droplets in NIH3T3 cells [14].
  • We show that directed mutations of residues at a particular corner of the gamma chain prevent recruitment to the TGN in cells and diminish PI-4-P-dependent, but not Arf1-dependent, liposome binding in vitro [15].
  • TGN localization of AP-1 depends on the small GTPase, Arf1, and the phosphoinositide, PI-4-P [15].
  • 3A specifically inhibits the function of GBF1, a guanine nucleotide exchange factor for Arf1, by interacting with its N terminus [10].
  • The present study showed that the GDP-bound ARF1 induces dissociation of ADRP from the LD surface, and that LD is a target of BFA action [16].

Enzymatic interactions of Arf1

  • Compared to wild-type Arf1, Arf1 with the amino terminal 13 ([Delta13]Arf1) and 17 amino acids ([Delta17]Arf1) deleted had 200- and 4000-fold reduced interaction with ASAP1 and 150-fold reduced interaction with AGAP1 [17].

Regulatory relationships of Arf1


Other interactions of Arf1

  • Taken together, the data suggest that the activation of Arf1-dependent PLD1 occurs in LDs and may be involved in their physiological function [14].
  • Differences between AGAP1, ASAP1 and Arf GAP1 in substrate recognition: interaction with the N-terminus of Arf1 [17].
  • Finally, the role of small GTP-binding proteins in the assembly of focal adhesions is discussed, along with our recent studies using streptolysin-O-permeabilized Swiss 3T3 cells which suggest that the GTP-binding protein ADP-ribosylation factor-1 (ARF-1) is important in targeting the protein paxillin to focal adhesions [19].
  • 7. Brefeldin A, an inhibitor of a factor which stimulates nucleotide exchange activity on the 21 kDa ADP-ribosylation factor, ARF, reduced LPS- and IFN gamma-induced NOS activity by approximately 80% [20].

Analytical, diagnostic and therapeutic context of Arf1


  1. A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Nagai, H., Kagan, J.C., Zhu, X., Kahn, R.A., Roy, C.R. Science (2002) [Pubmed]
  2. Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites. Kagan, J.C., Roy, C.R. Nat. Cell Biol. (2002) [Pubmed]
  3. ARF1 mediates paxillin recruitment to focal adhesions and potentiates Rho-stimulated stress fiber formation in intact and permeabilized Swiss 3T3 fibroblasts. Norman, J.C., Jones, D., Barry, S.T., Holt, M.R., Cockcroft, S., Critchley, D.R. J. Cell Biol. (1998) [Pubmed]
  4. Expression of a dominant allele of human ARF1 inhibits membrane traffic in vivo. Zhang, C.J., Rosenwald, A.G., Willingham, M.C., Skuntz, S., Clark, J., Kahn, R.A. J. Cell Biol. (1994) [Pubmed]
  5. Arf1 dissociates from the clathrin adaptor GGA prior to being inactivated by Arf GTPase-activating proteins. Jacques, K.M., Nie, Z., Stauffer, S., Hirsch, D.S., Chen, L.X., Stanley, K.T., Randazzo, P.A. J. Biol. Chem. (2002) [Pubmed]
  6. A BAR domain in the N terminus of the Arf GAP ASAP1 affects membrane structure and trafficking of epidermal growth factor receptor. Nie, Z., Hirsch, D.S., Luo, R., Jian, X., Stauffer, S., Cremesti, A., Andrade, J., Lebowitz, J., Marino, M., Ahvazi, B., Hinshaw, J.E., Randazzo, P.A. Curr. Biol. (2006) [Pubmed]
  7. Interaction of Staufen1 with the 5' end of mRNA facilitates translation of these RNAs. Dugré-Brisson, S., Elvira, G., Boulay, K., Chatel-Chaix, L., Mouland, A.J., DesGroseillers, L. Nucleic Acids Res. (2005) [Pubmed]
  8. The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly. Liu, Y., Loijens, J.C., Martin, K.H., Karginov, A.V., Parsons, J.T. Mol. Biol. Cell (2002) [Pubmed]
  9. Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus. Vitale, N., Horiba, K., Ferrans, V.J., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  10. A viral protein that blocks Arf1-mediated COP-I assembly by inhibiting the guanine nucleotide exchange factor GBF1. Wessels, E., Duijsings, D., Niu, T.K., Neumann, S., Oorschot, V.M., de Lange, F., Lanke, K.H., Klumperman, J., Henke, A., Jackson, C.L., Melchers, W.J., van Kuppeveld, F.J. Dev. Cell (2006) [Pubmed]
  11. Vesicle budding from endoplasmic reticulum is involved in calsequestrin routing to sarcoplasmic reticulum of skeletal muscles. Nori, A., Bortoloso, E., Frasson, F., Valle, G., Volpe, P. Biochem. J. (2004) [Pubmed]
  12. Different domains of the AP-1 adaptor complex are required for Golgi membrane binding and clathrin recruitment. Traub, L.M., Kornfeld, S., Ungewickell, E. J. Biol. Chem. (1995) [Pubmed]
  13. Electrotransfer in differentiated myotubes: a novel, efficient procedure for functional gene transfer. Sandri, M., Bortoloso, E., Nori, A., Volpe, P. Exp. Cell Res. (2003) [Pubmed]
  14. Arf1-dependent PLD1 is localized to oleic acid-induced lipid droplets in NIH3T3 cells. Nakamura, N., Banno, Y., Tamiya-Koizumi, K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  15. Crystal structure of the clathrin adaptor protein 1 core. Heldwein, E.E., Macia, E., Wang, J., Yin, H.L., Kirchhausen, T., Harrison, S.C. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  16. ADRP is dissociated from lipid droplets by ARF1-dependent mechanism. Nakamura, N., Akashi, T., Taneda, T., Kogo, H., Kikuchi, A., Fujimoto, T. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  17. Differences between AGAP1, ASAP1 and Arf GAP1 in substrate recognition: interaction with the N-terminus of Arf1. Yoon, H.Y., Jacques, K., Nealon, B., Stauffer, S., Premont, R.T., Randazzo, P.A. Cell. Signal. (2004) [Pubmed]
  18. SNAP25, but not syntaxin 1A, recycles via an ARF6-regulated pathway in neuroendocrine cells. Aikawa, Y., Xia, X., Martin, T.F. Mol. Biol. Cell (2006) [Pubmed]
  19. Integrin-mediated cell adhesion: the cytoskeletal connection. Critchley, D.R., Holt, M.R., Barry, S.T., Priddle, H., Hemmings, L., Norman, J. Biochem. Soc. Symp. (1999) [Pubmed]
  20. Protein kinase C and tyrosine kinase pathways regulate lipopolysaccharide-induced nitric oxide synthase activity in RAW 264.7 murine macrophages. Paul, A., Pendreigh, R.H., Plevin, R. Br. J. Pharmacol. (1995) [Pubmed]
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