ARF5 explained
ADP-ribosylation factor 5 is a protein that in humans is encoded by the ARF5 gene.[1] [2]
ADP-ribosylation factor 5 (ARF5) 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). The members of each class share a common gene organization. The ARF5 gene spans approximately 3.2kb of genomic DNA and contains six exons and five introns.[2]
Interactions
ARF5 has been shown to interact with ARFIP2.[3] [4]
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 .
- 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 . 10.1073/pnas.87.3.1238 . 53446 . 1990PNAS...87.1238S . 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 .
- Helms JB, Palmer DJ, Rothman JE . Two distinct populations of ARF bound to Golgi membranes . J. Cell Biol. . 121 . 4 . 751–60 . 1993 . 8491770 . 10.1083/jcb.121.4.751 . 2119793 .
- 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 .
- McGuire RE, Daiger SP, Green ED . Localization and characterization of the human ADP-ribosylation factor 5 (ARF5) gene . Genomics . 41 . 3 . 481–4 . 1997 . 9169151 . 10.1006/geno.1997.4689 .
- Andreev J, Simon JP, Sabatini DD . Identification of a New Pyk2 Target Protein with Arf-GAP Activity . Mol. Cell. Biol. . 19 . 3 . 2338–50 . 1999 . 10022920 . 10.1128/MCB.19.3.2338. 84026 . etal.
- Honda A, Nogami M, Yokozeki T . Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation . Cell . 99 . 5 . 521–32 . 1999 . 10589680 . 10.1016/S0092-8674(00)81540-8 . 10031591 . etal. free .
- Shin OH, Ross AH, Mihai I, Exton JH . Identification of arfophilin, a target protein for GTP-bound class II ADP-ribosylation factors . J. Biol. Chem. . 274 . 51 . 36609–15 . 2000 . 10593962 . 10.1074/jbc.274.51.36609 . free .
- Kondo A, Hashimoto S, Yano H . A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein Activity, Is Involved in Paxillin Recruitment to Focal Adhesions and Cell Migration . Mol. Biol. Cell . 11 . 4 . 1315–27 . 2000 . 10749932 . 10.1091/mbc.11.4.1315. 14849 . etal.
- Nevrivy DJ, Peterson VJ, Avram D . 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 . etal. free .
- Shin OH, Couvillon AD, Exton JH . Arfophilin is a common target of both class II and class III ADP-ribosylation factors . Biochemistry . 40 . 36 . 10846–52 . 2001 . 11535061 . 10.1021/bi0107391 .
- Austin C, Boehm M, Tooze SA . Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3 . Biochemistry . 41 . 14 . 4669–77 . 2002 . 11926829 . 10.1021/bi016064j .
- Strausberg RL, Feingold EA, Grouse LH . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . etal. 2002PNAS...9916899M . free .
- Scherer SW, Cheung J, MacDonald JR . Human Chromosome 7: DNA Sequence and Biology . Science . 300 . 5620 . 767–72 . 2003 . 12690205 . 10.1126/science.1083423 . 2882961 . etal. 2003Sci...300..767S .
- Gerhard DS, Wagner L, Feingold EA . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 . etal.
- Rual JF, Venkatesan K, Hao T . Towards a proteome-scale map of the human protein-protein interaction network . Nature . 437 . 7062 . 1173–8 . 2005 . 16189514 . 10.1038/nature04209 . etal. 2005Natur.437.1173R . 4427026 .
Notes and References
- Tsuchiya M, Price SR, Tsai SC, Moss J, Vaughan M . Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells . J Biol Chem . 266 . 5 . 2772–7 . March 1991. 10.1016/S0021-9258(18)49913-9 . 1993656 . free .
- Web site: Entrez Gene: ARF5 ADP-ribosylation factor 5.
- Kanoh . H . Williger B T. Exton J H . February 1997. Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes . J. Biol. Chem. . 272 . 9 . 5421–9 . UNITED STATES. 0021-9258. 9038142 . 10.1074/jbc.272.9.5421 . free .
- Shin . O H . Exton J H . August 2001. Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1 . Biochem. Biophys. Res. Commun. . 285 . 5 . 1267–73 . United States. 0006-291X. 11478794 . 10.1006/bbrc.2001.5330 .