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ARF1  -  ADP-ribosylation factor 1

Bos taurus

 
 
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High impact information on ARF1

  • This study shows that coatomer couples sorting signal recognition to the GTP hydrolysis reaction on ARF1 [1].
  • Unexpectedly, we find that the GTPgammaS-dependent activator of PI(4)P5Kalpha is the small G protein ADP-ribosylation factor (ARF) and that the activation strictly requires phosphatidic acid, the product of phospholipase D (PLD) [2].
  • The coat proteins required for budding COP-coated vesicles from Golgi membranes, coatomer and ADP-ribosylation factor (ARF) protein, are shown to be required to reconstitute the orderly process of transport between Golgi cisternae in which fusion of transport vesicles begins only after budding ends [3].
  • Partial purification yielded an approximately 60-kDa BFA-insensitive GEP that enhanced binding of ARF1 and ARF3 to Golgi membranes [4].
  • In the presence of 0.6-0.8 mM MgCl2 and 1 mM EDTA, binding of guanosine 5'-[gamma[35S]thio]triphosphate ([35S]GTP gamma S) by ARF1 and ARF3 was equally high without and with GEP [4].
 

Biological context of ARF1

 

Anatomical context of ARF1

  • At the trans-Golgi network, clathrin coats containing AP-1 adaptor complexes are formed in an ARF1-dependent manner, generating vesicles transporting cargo proteins to endosomes [7].
  • GTPgammaS-stimulated lysis was reconstituted with ARF1 purified from bovine brain cytosol or recombinant ARF1 [8].
  • We have used the reconstitution of transport vesicle formation on isolated Golgi membranes to characterize mechanisms of ARF1 regulated actin polymerization [9].
  • These data imply that CaM stimulates the PLD activity of rabbit neutrophils in concert with ARF [10].
  • To investigate the role of ARF in regulated exocytosis, we have examined its intracellular distribution in cultured chromaffin cells by subcellular fractionation and immunoreplica analysis [11].
 

Associations of ARF1 with chemical compounds

  • AP-1 recruitment was found to be dependent on myristoylated ARF1, GTP or nonhydrolyzable GTP-analogs, tyrosine signals, and small amounts of phosphoinositides, most prominently phosphatidylinositol 4,5-bisphosphate, in the absence of any additional cytosolic or membrane bound proteins [7].
  • The ADP-ribosylation factor (ARF) is a 21-kDa GTP-binding protein that serves as the cofactor in the cholera toxin-catalyzed activation of the stimulatory guanine nucleotide-binding protein of adenylate cyclase (Gs) [5].
  • The retinal extract also stimulates guanosine 5'-3-O-(thio)-triphosphate (GTP gamma S) release from ARF1 in the presence of phospholipids, but in this case myristoylation of ARF is not required [12].
  • Vesicle formation was stimulated by supplemented clathrin, but inhibited by brefeldin A, consistent with the involvement of ARF1 and a brefeldin-sensitive guanine nucleotide exchange factor [13].
  • The role of the amino terminus in the actions of ADP-ribosylation factor 1 (ARF1) was examined by comparing wild type ARF1, a 13-residue NH2-terminal deletion mutant ([delta 13]ARF1), and a 17-residue NH2-terminal deletion mutant ([delta 17]ARF1) [14].
 

Other interactions of ARF1

 

Analytical, diagnostic and therapeutic context of ARF1

  • The recombinant Arf1 was compared with purified bovine brain Arf and shown to be nearly identical with respect to immunoblotting, guanine nucleotide binding, GTP hydrolysis, and cholera toxin cofactor activities [17].

References

  1. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Goldberg, J. Cell (2000) [Pubmed]
  2. Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein ARF6 in membrane ruffle formation. Honda, A., Nogami, M., Yokozeki, T., Yamazaki, M., Nakamura, H., Watanabe, H., Kawamoto, K., Nakayama, K., Morris, A.J., Frohman, M.A., Kanaho, Y. Cell (1999) [Pubmed]
  3. ADP-ribosylation factor and coatomer couple fusion to vesicle budding. Elazar, Z., Orci, L., Ostermann, J., Amherdt, M., Tanigawa, G., Rothman, J.E. J. Cell Biol. (1994) [Pubmed]
  4. Purification and characterization of a guanine nucleotide-exchange protein for ADP-ribosylation factor from spleen cytosol. Tsai, S.C., Adamik, R., Moss, J., Vaughan, M. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  5. Sequences of the bovine and yeast ADP-ribosylation factor and comparison to other GTP-binding proteins. Sewell, J.L., Kahn, R.A. Proc. Natl. Acad. Sci. U.S.A. (1988) [Pubmed]
  6. Aluminum fluoride acts on the reversibility of ARF1-dependent coat protein binding to Golgi membranes. Finazzi, D., Cassel, D., Donaldson, J.G., Klausner, R.D. J. Biol. Chem. (1994) [Pubmed]
  7. ARF1.GTP, tyrosine-based signals, and phosphatidylinositol 4,5-bisphosphate constitute a minimal machinery to recruit the AP-1 clathrin adaptor to membranes. Crottet, P., Meyer, D.M., Rohrer, J., Spiess, M. Mol. Biol. Cell (2002) [Pubmed]
  8. ARF-induced lysosomal lysis in vitro. Arai, K., Matsuda, T., Sai, Y., Ohkuma, S. J. Biochem. (1998) [Pubmed]
  9. In vitro reconstitution of ARF-regulated cytoskeletal dynamics on Golgi membranes. Chen, J.L., Xu, W., Stamnes, M. Meth. Enzymol. (2005) [Pubmed]
  10. Augmentation by calmodulin of ADP-ribosylation factor-stimulated phospholipase D activity in permeabilized rabbit peritoneal neutrophils. Takahashi, K., Tago, K., Okano, H., Ohya, Y., Katada, T., Kanaho, Y. J. Immunol. (1996) [Pubmed]
  11. Regulated exocytosis in chromaffin cells. A potential role for a secretory granule-associated ARF6 protein. Galas, M.C., Helms, J.B., Vitale, N., Thiersé, D., Aunis, D., Bader, M.F. J. Biol. Chem. (1997) [Pubmed]
  12. Myristoylation-facilitated binding of the G protein ARF1GDP to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor. Franco, M., Chardin, P., Chabre, M., Paris, S. J. Biol. Chem. (1996) [Pubmed]
  13. In vitro formation of recycling vesicles from endosomes requires adaptor protein-1/clathrin and is regulated by rab4 and the connector rabaptin-5. Pagano, A., Crottet, P., Prescianotto-Baschong, C., Spiess, M. Mol. Biol. Cell (2004) [Pubmed]
  14. The amino terminus of ADP-ribosylation factor (ARF) 1 is essential for interaction with Gs and ARF GTPase-activating protein. Randazzo, P.A., Terui, T., Sturch, S., Kahn, R.A. J. Biol. Chem. (1994) [Pubmed]
  15. Parathyroid hormone (PTH) secretion: stimulation of PTH secretion by a peptide derived from the adenosine diphosphate-ribosylation factor. Newman, L., Drees, B., Forte, L., Hamilton, J. Endocrinology (1994) [Pubmed]
  16. Isolation, cloning, and characterization of brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factor. Pacheco-Rodriguez, G., Moss, J., Vaughan, M. Meth. Enzymol. (2001) [Pubmed]
  17. Nucleotide binding and cofactor activities of purified bovine brain and bacterially expressed ADP-ribosylation factor. Weiss, O., Holden, J., Rulka, C., Kahn, R.A. J. Biol. Chem. (1989) [Pubmed]
 
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