Arf GTPase-activating proteins

Randazzo PA, Terui T, Sturch S, et al. (1994) The amino terminus of ADP-ribosylation factor (ARF) 1 is essential for the interaction of Gs and ARF GTPase-activating protein. In J. Biol. Chem. 269 29490-29494. 

Brown, M. T., Andrade, J., Radhakrishna, H., Donaldson, J. G., Cooper, J. A., and Randazzo, P. A. (1998). ASAPl, a phosphoUpid-dependent Arf GTPase-activating protein that associates with and is phosphorylated by Src. Mol. Cell. Biol. 18,7038-7051. 

Cassel, D. (2003). Arf GTPase-activating protein 1. In Arf Family GTPases (R. A. Kahn, ed.), pp. 137-158. Kluwer Academic Publishers, Dordrecht. 

Randazzo, P. A., Miura, K., and Jackson, T. R. (2001). Assay and purification of phosphoinositide-dependent ADP-ribosylation factor (ARF) GTPase activating proteins. Regulators and effectors of small GTPases. Meth. Enzymol. 329, 343-354. 

Paris, S., Longhi, R., Santambrogio, P., and de Curtis, I. (2003). Leucine-zipper-mediated homo- and hetero-dimerization of GIT family p95-ARF GTPase-activating protein, PIX-, paxillin-interacting proteins 1 and 2. Biochem. J. 372, 391-398. 

Kruljac-Letunic, A., Moelleken, J., Kallin, A., Wieland, F., and Blaukat, A. (2003). The tyrosine kinase Pyk2 regulates Arfl activity by phosphorylation and inhibition of the Arf-GTPase-activating protein ASAPl. J. Biol. Chem. 278, 29560-29570. 

ArfGap Putative GTPase activating proteins for the small GTPase, ARF E(MFP) 6(6) 8(8) ... 

Ding, M., Vitale, N., Tsai, S. C., Adamik, R., Moss, J., and Vaughan, M. (1996). Characterization of a GTPase-activating protein that stimulates GTP hydrolysis by both ADP-ribosylation factor (ARF) and ARF-like proteins. J. Biol. Chem. 271, 24005-24009. 

Cholera toxin catalyzes the ADP-ribosylation of a specific arginine residue in G and Gat. This covalent modification inhibits the intrinsic GTPase activity of these a subunits and thereby freezes them in their activated, or free, state (Fig. 19-1C). By this mechanism, cholera toxin stimulates adenylyl cyclase activity and photoreceptor transduction mechanisms. The ability of cholera toxin to ADP-ribosylate G may require the presence of a distinct protein, ADP-ribosylation factor (ARF). ARF, which is itself a small G protein (Table 19-2), also is ADP-ribosylated by cholera toxin. ARF is implicated in controlling membrane vesicle trafficking (see Ch. 9). 

Pacheco-Rodriguez et al, 1998 Vitale et al., 2000). Interaction with the ARF domain of ARDl required lysine 91 in the cytohesin-1 See domain (Vitale et ai, 2000), which is not within the sequences (motifs 1 and 2) that are critical for GEP activity. The 64-kDa ARD-1 was discovered and cloned because of its C-terminal 18-kDa ARF domain (Mishima et al., 1993). Its GTPase-activating domain was later recognized (Vitale et al., 1996). The molecular structure of ARDl identified it as a member of the TRIM (Tripartite motif) or RBCC (RING, B-Box, coiled-coil) protein family and Vichi et ai, (2005) demonstrated E3 ubiquitin ligase activity in the N-terminal part of the molecule. 

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