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Gene Review

ARF3  -  ADP-ribosylation factor 3

Homo sapiens

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High impact information on ARF3

  • This factor was purified and identified as two small GTP-binding proteins, ARF1 and ARF3 [1].
  • Brefeldin A-inhibited guanine nucleotide-exchange proteins (BIG) 1 and BIG2 activate human ADP-ribosylation factors (ARF) 1 and ARF3 by catalyzing the replacement of ARF-bound GDP with GTP to regulate Golgi vesicular transport [2].
  • 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 [3].
  • The ability of certain mutants of ARF3 to alter Golgi morphology without changes in PLD1 activity or COP-I binding is interpreted as evidence for at least one additional, currently unidentified, effector for ARF action at the Golgi [4].
  • Arfaptin 1, a approximately 39-kDa protein based on the deduced amino acid sequence, had been initially identified in a yeast two-hybrid screen using dominant active ARF3 (Q71L) as bait with an HL-60 cDNA library [5].

Biological context of ARF3

  • Employing yeast two-hybrid screening of an HL60 cDNA library using a constitutively active mutant of ARF3 (ARF3.Q71L), as a probe, we have identified a cDNA encoding a novel protein with a calculated molecular mass of 38.6 kDa, which we have named arfaptin 1 [6].
  • Sequences of two overlapping genomic clones indicated that the ARF 3 gene spans approximately 18.3 kb and contains five exons and four introns [7].
  • The latter encodes the COOH-terminal 53 amino acids of ARF 3 and contains greater than 2500 base pairs of untranslated DNA [7].
  • The 1.2-kb ARF 3 mRNA is shown to arise by use of an alternative polyadenylation signal (AACAAA) at nucleotide 1091 within the ARF 3 cDNA [7].
  • A screen for mutations in Arf3 that specifically lost the ability to bind MKLP1 identified 10 of 14 point mutations in the GTP-sensitive switch I or switch II regions of Arf3 [8].

Anatomical context of ARF3

  • The relative expression of ARFs in endothelial cells thus differs from that in neuronal tissues where it had been found that ARF3 is the predominant species [9].
  • In addition, the ARF3 protein was developmentally regulated in the mammary gland with the highest levels in virgin and post-weaning glands [10].
  • Together, these findings suggest for the first time that stimulation of ARF3 expression, subcellular redistribution and interaction with acetylated histone H3 may play a role in the action of HRG in mammary epithelial cells [10].
  • Also, HRG triggered a rapid redistribution of ARF3, first to cell membranes and then to the nuclear compartment, where ARF3 colocalized with acetylated histone H3 in discrete regions [10].
  • However, addition of myristoylated ARF3 (myrARF3) increases the association of arfaptin 1 with the membranes, suggesting that arfaptin 1 and ARF form a complex on the Golgi [11].

Associations of ARF3 with chemical compounds

  • In contrast, the NH2 termini of Group I ARFs (ARF1 and ARF3), although fully deformylated, undergo only partial methionine cleavage [12].
  • 5. The enzyme was inhibited by oleate and activated by the small G proteins ARF3 and RhoA in the presence of guanosine 5'-3-O-(thio)triphosphate [13].
  • In the ARF 3 gene in contrast to those of other GTP-binding proteins, the sequence NKXD (which is thought to contribute to the specificity of interaction with the guanine ring) is divided between exons 4 and 5 [7].

Physical interactions of ARF3

  • Golgi incubated with GTP[gamma S] and purified ARF 1 or 3 bound more ARF 1 than ARF 3 [3].
  • Further deletion mapping allowed the identification of an 88 amino acid Arf3 binding domain in the C-terminus of MKLP1 [8].

Other interactions of ARF3

  • It activated native ARF (mixture of ARF1 and ARF3) more effectively than it did any of the nonmyristoylated recombinant ARFs [14].
  • In this study, we define sites of interaction between LTA and human ARF3 [15].
  • Neither synergistic interactions between ARF3 and RhoA nor between these G proteins and PKC-alpha or -betaII were observed [13].
  • The C-terminal domain of MKLP1 was expressed and purified from bacteria as a GST fusion protein and shown to bind Arf3 in a GTP-dependent fashion [8].
  • Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin [7].

Analytical, diagnostic and therapeutic context of ARF3


  1. Phospholipase D: a downstream effector of ARF in granulocytes. Cockcroft, S., Thomas, G.M., Fensome, A., Geny, B., Cunningham, E., Gout, I., Hiles, I., Totty, N.F., Truong, O., Hsuan, J.J. Science (1994) [Pubmed]
  2. BIG1, a brefeldin A-inhibited guanine nucleotide-exchange protein, is required for correct glycosylation and function of integrin beta1. Shen, X., Hong, M.S., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (2007) [Pubmed]
  3. 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]
  4. Effects of activated ADP-ribosylation factors on Golgi morphology require neither activation of phospholipase D1 nor recruitment of coatomer. Kuai, J., Boman, A.L., Arnold, R.S., Zhu, X., Kahn, R.A. J. Biol. Chem. (2000) [Pubmed]
  5. Effects of arfaptin 1 on guanine nucleotide-dependent activation of phospholipase D and cholera toxin by ADP-ribosylation factor. Tsai, S.C., Adamik, R., Hong, J.X., Moss, J., Vaughan, M., Kanoh, H., Exton, J.H. J. Biol. Chem. (1998) [Pubmed]
  6. Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. Kanoh, H., Williger, B.T., Exton, J.H. J. Biol. Chem. (1997) [Pubmed]
  7. Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin. Tsai, S.C., Haun, R.S., Tsuchiya, M., Moss, J., Vaughan, M. J. Biol. Chem. (1991) [Pubmed]
  8. Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion. Boman, A.L., Kuai, J., Zhu, X., Chen, J., Kuriyama, R., Kahn, R.A. Cell Motil. Cytoskeleton (1999) [Pubmed]
  9. Expression in human endothelial cells of ADP-ribosylation factors, 20-kDa guanine nucleotide-binding proteins involved in the initiation of vesicular transport. Lee, C.M., Stevens, L.A., Hsu, H.C., Tsai, S.C., Lee, Y.T., Moss, J., Vaughan, M. J. Mol. Cell. Cardiol. (1996) [Pubmed]
  10. Heregulin promotes expression and subcellular redistribution of ADP-ribosylation factor 3. Li, F., Mandal, M., Mishra, S.K., Barnes, C.J., Kumar, R. FEBS Lett. (2002) [Pubmed]
  11. Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D. Williger, B.T., Provost, J.J., Ho, W.T., Milstine, J., Exton, J.H. FEBS Lett. (1999) [Pubmed]
  12. 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]
  13. Characterization of a rat brain phospholipase D isozyme. Min, D.S., Park, S.K., Exton, J.H. J. Biol. Chem. (1998) [Pubmed]
  14. Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. Togawa, A., Morinaga, N., Ogasawara, M., Moss, J., Vaughan, M. J. Biol. Chem. (1999) [Pubmed]
  15. ARF binds the C-terminal region of the Escherichia coli heat-labile toxin (LTA1) and competes for the binding of LTA2. Zhu, X., Kim, E., Boman, A.L., Hodel, A., Cieplak, W., Kahn, R.A. Biochemistry (2001) [Pubmed]
  16. Analysis of 148 kb of genomic DNA around the wnt1 locus of Fugu rubripes. Gellner, K., Brenner, S. Genome Res. (1999) [Pubmed]
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