ARF1
ADP-ribosylation factor 1 is a protein that in humans is encoded by the ARF1 gene.[1]
ADP-ribosylation factor 1 (ARF1) is a member of the human ARF gene family. The family members encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking as activators of phospholipase D. The gene products, including 6 ARF proteins and 11 ARF-like proteins, constitute a 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 ARF1 protein is localized to the Golgi apparatus and has a central role in intra-Golgi transport. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene.[2]
Interactions
ARF1 has been shown to interact with GGA3,[3][4] PLD2,[5][6] COPB1[7][8] and Muscarinic acetylcholine receptor M3.[9]
References
- ^ Lee CM, Haun RS, Tsai SC, Moss J, Vaughan M (Jun 1992). "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. PMID 1577740.
- ^ "Entrez Gene: ARF1 ADP-ribosylation factor 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=375.
- ^ Dell'Angelica, E C; Puertollano R, Mullins C, Aguilar R C, Vargas J D, Hartnell L M, Bonifacino J S (Apr. 2000). "GGAs: a family of ADP ribosylation factor-binding proteins related to adaptors and associated with the Golgi complex". J. Cell Biol. (UNITED STATES) 149 (1): 81–94. doi:10.1083/jcb.149.1.81. ISSN 0021-9525. PMC 2175099. PMID 10747089. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2175099.
- ^ Puertollano, R; Randazzo P A, Presley J F, Hartnell L M, Bonifacino J S (Apr. 2001). "The GGAs promote ARF-dependent recruitment of clathrin to the TGN". Cell (United States) 105 (1): 93–102. doi:10.1016/S0092-8674(01)00299-9. ISSN 0092-8674. PMID 11301005.
- ^ Lee, S; Park J B, Kim J H, Kim Y, Kim J H, Shin K J, Lee J S, Ha S H, Suh P G, Ryu S H (Jul. 2001). "Actin directly interacts with phospholipase D, inhibiting its activity". J. Biol. Chem. (United States) 276 (30): 28252–60. doi:10.1074/jbc.M008521200. ISSN 0021-9258. PMID 11373276.
- ^ Park, J B; Kim J H, Kim Y, Ha S H, Yoo J S, Du G, Frohman M A, Suh P G, Ryu S H (Jul. 2000). "Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner". J. Biol. Chem. (UNITED STATES) 275 (28): 21295–301. doi:10.1074/jbc.M002463200. ISSN 0021-9258. PMID 10801846.
- ^ Fischer, K D; Helms J B, Zhao L, Wieland F T (Apr. 2000). "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods (UNITED STATES) 20 (4): 455–64. doi:10.1006/meth.2000.0958. ISSN 1046-2023. PMID 10720466.
- ^ Eugster, A; Frigerio G, Dale M, Duden R (Aug. 2000). "COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAP". EMBO J. (ENGLAND) 19 (15): 3905–17. doi:10.1093/emboj/19.15.3905. ISSN 0261-4189. PMC 306616. PMID 10921873. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=306616.
- ^ Mitchell, Rory; Robertson Derek N, Holland Pamela J, Collins Daniel, Lutz Eve M, Johnson Melanie S (Sep. 2003). "ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor". J. Biol. Chem. (United States) 278 (36): 33818–30. doi:10.1074/jbc.M305825200. ISSN 0021-9258. PMID 12799371.
Further reading
- Serafini T, Orci L, Amherdt M, et al. (1991). "ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein.". Cell 67 (2): 239–53. doi:10.1016/0092-8674(91)90176-Y. PMID 1680566.
- Kahn RA, Kern FG, Clark J, et al. (1991). "Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins.". J. Biol. Chem. 266 (4): 2606–14. PMID 1899243.
- Stearns T, Willingham MC, Botstein D, Kahn RA (1990). "ADP-ribosylation factor is functionally and physically associated with the Golgi complex.". Proc. Natl. Acad. Sci. U.S.A. 87 (3): 1238–42. doi:10.1073/pnas.87.3.1238. PMC 53446. PMID 2105501. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=53446.
- Bobak DA, Nightingale MS, Murtagh JJ, et al. (1989). "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. doi:10.1073/pnas.86.16.6101. PMC 297783. PMID 2474826. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=297783.
- Greasley SE, Jhoti H, Teahan C, et al. (1995). "The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms.". Nat. Struct. Biol. 2 (9): 797–806. doi:10.1038/nsb0995-797. PMID 7552752.
- Welsh CF, Moss J, Vaughan M (1995). "ADP-ribosylation factors: a family of approximately 20-kDa guanine nucleotide-binding proteins that activate cholera toxin.". Mol. Cell. Biochem. 138 (1–2): 157–66. doi:10.1007/BF00928458. PMID 7898460.
- Greasley S, Jhoti H, Fensome AC, et al. (1995). "Crystallization and preliminary X-ray diffraction studies on ADP-ribosylation factor 1". J. Mol. Biol. 244 (5): 651–3. doi:10.1006/jmbi.1994.1759. PMID 7990146.
- Amor JC, Harrison DH, Kahn RA, Ringe D (1995). "Structure of the human ADP-ribosylation factor 1 complexed with GDP". Nature 372 (6507): 704–8. doi:10.1038/372704a0. PMID 7990966.
- Dascher C, Balch WE (1994). "Dominant inhibitory mutants of ARF1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus". J. Biol. Chem. 269 (2): 1437–48. PMID 8288610.
- Rümenapp U, Geiszt M, Wahn F, et al. (1996). "Evidence for ADP-ribosylation-factor-mediated activation of phospholipase D by m3 muscarinic acetylcholine receptor". Eur. J. Biochem. 234 (1): 240–4. doi:10.1111/j.1432-1033.1995.240_c.x. PMID 8529647.
- Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Hirai M, Kusuda J, Hashimoto K (1997). "Assignment of human ADP ribosylation factor (ARF) genes ARF1 and ARF3 to chromosomes 1q42 and 12q13, respectively". Genomics 34 (2): 263–5. doi:10.1006/geno.1996.0283. PMID 8661066.
- Kanoh H, Williger BT, Exton JH (1997). "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes". J. Biol. Chem. 272 (9): 5421–9. doi:10.1074/jbc.272.9.5421. PMID 9038142.
- Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139146.
- Shome K, Vasudevan C, Romero G (1997). "ARF proteins mediate insulin-dependent activation of phospholipase D". Curr. Biol. 7 (6): 387–96. doi:10.1016/S0960-9822(06)00186-2. PMID 9197239.
- Frank S, Upender S, Hansen SH, Casanova JE (1998). "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6". J. Biol. Chem. 273 (1): 23–7. doi:10.1074/jbc.273.1.23. PMID 9417041.
- Betz SF, Schnuchel A, Wang H, et al. (1998). "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 7909–14. doi:10.1073/pnas.95.14.7909. PMC 20903. PMID 9653114. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=20903.
- Kim JH, Lee SD, Han JM, et al. (1998). "Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA". FEBS Lett. 430 (3): 231–5. doi:10.1016/S0014-5793(98)00661-9. PMID 9688545.
- Huber I, Cukierman E, Rotman M, et al. (1998). "Requirement for both the amino-terminal catalytic domain and a noncatalytic domain for in vivo activity of ADP-ribosylation factor GTPase-activating protein". J. Biol. Chem. 273 (38): 24786–91. doi:10.1074/jbc.273.38.24786. PMID 9733781.
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PDB gallery
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1hur: HUMAN ADP-RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP, FULL LENGTH NON-MYRISTOYLATED
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1j2j: Crystal structure of GGA1 GAT N-terminal region in complex with ARF1 GTP form
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1o3y: Crystal structure of mouse ARF1 (delta17-Q71L), GTP form
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1r8q: FULL-LENGTH ARF1-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN
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1r8s: ARF1[DELTA1-17]-GDP IN COMPLEX WITH A SEC7 DOMAIN CARRYING THE MUTATION OF THE CATALYTIC GLUTAMATE TO LYSINE
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1re0: Structure of ARF1-GDP bound to Sec7 domain complexed with Brefeldin A
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1rrf: NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, MONOMERIC CRYSTAL FORM
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1rrg: NON-MYRISTOYLATED RAT ADP-RIBOSYLATION FACTOR-1 COMPLEXED WITH GDP, DIMERIC CRYSTAL FORM
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1s9d: ARF1[DELTA 1-17]-GDP-MG IN COMPLEX WITH BREFELDIN A AND A SEC7 DOMAIN
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1u81: Delta-17 Human ADP Ribosylation Factor 1 Complexed with GDP
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2j59: CRYSTAL STRUCTURE OF THE ARF1:ARHGAP21-ARFBD COMPLEX
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