ARF1 Information & ARF1 Links at HealthHaven.com

ADP-ribosylation factor 1
	PDB rendering based on 1hur.
Available structures
	1hur, 1j2j, 1o3y, 1r8q, 1r8s, 1re0, 1rrf, 1rrg, 1s9d, 1u81, 2j59
Identifiers
Symbols	ARF1;
External IDs	OMIM: 103180 MGI: 99431 HomoloGene: 56086
Gene ontology
Molecular function	• nucleotide binding; • GTPase activity; • receptor signaling protein activity; • protein binding; • GTP binding;
Cellular component	• intracellular; • plasma membrane;
Biological process	• ER to Golgi vesicle-mediated transport; • small GTPase mediated signal transduction; • protein transport;
RNA expression pattern
	More reference expression data
Orthologs
NP_001019397 (protein)	NP_031502 (protein)

edit

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]

[edit] Interactions

ARF1 has been shown to interact with GGA3,^[3]^[4] PLD2,^[5]^[6] COPB1^[7]^[8] and Muscarinic acetylcholine receptor M3.^[9]

[edit] 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. ISSN 0021-9525. PMID 10747089.
^ 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. 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. PMID 10921873.
^ 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.

[edit] 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. PMID 2105501.
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. PMID 2474826.
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. PMID 9110174.
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. PMID 9653114.
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.

This article on a gene on chromosome 1 is a stub. You can help Wikipedia by expanding it.

[pmid1577740-0] 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.

[1] "Entrez Gene: ARF1 ADP-ribosylation factor 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=375.

[pmid10747089-2] 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. ISSN 0021-9525. PMID 10747089.

[pmid11301005-3] 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. ISSN 0092-8674. PMID 11301005.

[pmid11373276-4] 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.

[pmid10801846-5] 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.

[pmid10720466-6] 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.

[pmid10921873-7] 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. PMID 10921873.

[pmid12799371-8] 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.

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