ARF3 explained
ADP-ribosylation factor 3 is a protein that in humans is encoded by the ARF3 gene.[1] [2]
Function
ADP-ribosylation factor 3 (ARF3) is a member of the human ARF gene family. These 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 gene products include 6 ARF proteins and 11 ARF-like proteins and constitute 1 family of the RAS superfamily. The ARF proteins are categorized as class I (ARF1, ARF2, and ARF3), class II (ARF4 and ARF5) and class III (ARF6) and members of each class share a common gene organization. The ARF3 gene contains five exons and four introns.[2]
Interactions
ARF3 has been shown to interact with:
Further reading
- Lee FJ, Moss J, Vaughan M . Human and Giardia ADP-ribosylation factors (ARFs) complement ARF function in Saccharomyces cerevisiae . J. Biol. Chem. . 267 . 34 . 24441–5 . 1992 . 10.1016/S0021-9258(18)35786-7 . 1447192 . free .
- Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M . Characterization of the human gene encoding ADP-ribosylation factor 1, a guanine nucleotide-binding activator of cholera toxin . J. Biol. Chem. . 267 . 13 . 9028–34 . 1992 . 10.1016/S0021-9258(19)50383-0 . 1577740 . free .
- Tsai SC, Haun RS, Tsuchiya M, Moss J, Vaughan M . Isolation and characterization of the human gene for ADP-ribosylation factor 3, a 20-kDa guanine nucleotide-binding protein activator of cholera toxin . J. Biol. Chem. . 266 . 34 . 23053–9 . 1991 . 10.1016/S0021-9258(18)54462-8 . 1744102 . free .
- Stearns T, Willingham MC, Botstein D, Kahn RA . ADP-ribosylation factor is functionally and physically associated with the Golgi complex . Proc. Natl. Acad. Sci. U.S.A. . 87 . 3 . 1238–42 . 1990 . 2105501 . 53446 . 10.1073/pnas.87.3.1238 . 1990PNAS...87.1238S . free .
- Bobak DA, Nightingale MS, Murtagh JJ, Price SR, Moss J, Vaughan M . Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin . Proc. Natl. Acad. Sci. U.S.A. . 86 . 16 . 6101–5 . 1989 . 2474826 . 297783 . 10.1073/pnas.86.16.6101 . 1989PNAS...86.6101B . free .
- Orcl L, Palmer DJ, Amherdt M, Rothman JE . Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins from the cytosol . Nature . 364 . 6439 . 732–4 . 1993 . 8355790 . 10.1038/364732a0 . 1993Natur.364..732O . 4348442 .
- Haun RS, Moss J, Vaughan M . Characterization of the human ADP-ribosylation factor 3 promoter. Transcriptional regulation of a TATA-less promoter . J. Biol. Chem. . 268 . 12 . 8793–800 . 1993 . 10.1016/S0021-9258(18)52944-6 . 8473323 . free .
- Helms JB, Palmer DJ, Rothman JE . Two distinct populations of ARF bound to Golgi membranes . J. Cell Biol. . 121 . 4 . 751–60 . 1993 . 8491770 . 2119793 . 10.1083/jcb.121.4.751 .
- Hosaka M, Toda K, Takatsu H, Torii S, Murakami K, Nakayama K . Structure and intracellular localization of mouse ADP-ribosylation factors type 1 to type 6 (ARF1-ARF6) . J. Biochem. . 120 . 4 . 813–9 . 1996 . 8947846 . 10.1093/oxfordjournals.jbchem.a021484 .
- Kanoh H, Williger BT, Exton JH . Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes . J. Biol. Chem. . 272 . 9 . 5421–9 . 1997 . 9038142 . 10.1074/jbc.272.9.5421 . free.
- Williger BT, Provost JJ, Ho WT, Milstine J, Exton JH . Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D . FEBS Lett. . 454 . 1–2 . 85–9 . 1999 . 10413101 . 10.1016/S0014-5793(99)00771-1 . 40655171 .
- Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA . Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion . Cell Motil. Cytoskeleton . 44 . 2 . 119–32 . 1999 . 10506747 . 10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C .
- Takeya R, Takeshige K, Sumimoto H . Interaction of the PDZ domain of human PICK1 with class I ADP-ribosylation factors . Biochem. Biophys. Res. Commun. . 267 . 1 . 149–55 . 2000 . 10623590 . 10.1006/bbrc.1999.1932 .
- Boman AL, ((Zhang Cj)), Zhu X, Kahn RA . A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi . Mol. Biol. Cell . 11 . 4 . 1241–55 . 2000 . 10749927 . 14844 . 10.1091/mbc.11.4.1241 .
- Nevrivy DJ, Peterson VJ, Avram D, Ishmael JE, Hansen SG, Dowell P, Hruby DE, Dawson MI, Leid M . Interaction of GRASP, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors . J. Biol. Chem. . 275 . 22 . 16827–36 . 2000 . 10828067 . 10.1074/jbc.275.22.16827 . free .
- Zhdankina O, Strand NL, Redmond JM, Boman AL . Yeast GGA proteins interact with GTP-bound Arf and facilitate transport through the Golgi . Yeast . 18 . 1 . 1–18 . 2001 . 11124697 . 10.1002/1097-0061(200101)18:1<1::AID-YEA644>3.0.CO;2-5 . 10348751 . free .
- Irobi J, Nelis E, Verhoeven K, De Vriendt E, Dierick I, De Jonghe P, Van Broeckhoven C, Timmerman V . Mutation analysis of 12 candidate genes for distal hereditary motor neuropathy type II (distal HMN II) linked to 12q24.3 . J. Peripher. Nerv. Syst. . 7 . 2 . 87–95 . 2002 . 12090300 . 10.1046/j.1529-8027.2002.02014.x . 8453412 .
- Li F, Mandal M, Mishra SK, Barnes CJ, Kumar R . Heregulin promotes expression and subcellular redistribution of ADP-ribosylation factor 3 . FEBS Lett. . 524 . 1–3 . 49–53 . 2002 . 12135740 . 10.1016/S0014-5793(02)02994-0 . 36764648 .
- Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O . ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization . Mol. Biol. Cell . 13 . 9 . 3078–95 . 2002 . 12221117 . 124144 . 10.1091/mbc.E02-02-0078 .
Notes and References
- Hirai M, Kusuda J, Hashimoto K . Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively . Genomics . 34 . 2 . 263–5 . June 1996 . 8661066 . 10.1006/geno.1996.0283 .
- Web site: Entrez Gene: ARF3 ADP-ribosylation factor 3.
- Williger BT, Provost JJ, Ho WT, Milstine J, Exton JH . Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D . FEBS Lett. . 454 . 1–2 . 85–9 . July 1999 . 10413101 . 10.1016/s0014-5793(99)00771-1. 40655171 .
- Kanoh H, Williger BT, Exton JH . Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes . J. Biol. Chem. . 272 . 9 . 5421–9 . February 1997 . 9038142 . 10.1074/jbc.272.9.5421. free.
- Boman AL, Salo PD, Hauglund MJ, Strand NL, Rensink SJ, Zhdankina O . ADP-ribosylation factor (ARF) interaction is not sufficient for yeast GGA protein function or localization . Mol. Biol. Cell . 13 . 9 . 3078–95 . September 2002 . 12221117 . 124144 . 10.1091/mbc.E02-02-0078 .
- Boman AL, ((Zhang Cj)), Zhu X, Kahn RA . A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi . Mol. Biol. Cell . 11 . 4 . 1241–55 . April 2000 . 10749927 . 14844 . 10.1091/mbc.11.4.1241.
- Boman AL, Kuai J, Zhu X, Chen J, Kuriyama R, Kahn RA . Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion . Cell Motil. Cytoskeleton . 44 . 2 . 119–32 . October 1999 . 10506747 . 10.1002/(SICI)1097-0169(199910)44:2<119::AID-CM4>3.0.CO;2-C .