ARF GTPase

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. 

Goldberg, J. (1998) Structural basis for activation of ARF GTPase mechanisms of guanine nucleotide exchange and GTP-my-ristoyl switching. Cell, 95, 237-248. 

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. 

Mossessova, E., Gulbis, J. M, and Goldberg, J. (1998). Structure of the guanine nucleotide exchange factor Sec7 domain of human amo and analysis of the interaction with ARF GTPase. CeU 92,415-423. 

Shin, H.-W., andNakayama, K. (2004). Guanine nucleotide-exchange factors for Arf GTPases Their diverse functions in membrane traffic. J. Biochem. (Tokyo) 136,761-767. 

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. 

In Vitro Arf GTPase Assay to Study the Modulation of ASAPl GAP Activity by Tyrosine Phosphorylation... 

Fig. 3. In vitro Arf-GTPas assay to measure the GAP activity of ASAPl. (A) The stoichiometry of ASAPl tyrosine phosphorylation can be increased by in vitro kinase reaction performed with purified Flag-ASAP1/Pyk2 complexes. This increase is followed by Western blotting with an anti-phosphotyrosine antibody (pY) and levels of Hag-ASAPl are controlled with an anti-Flag antibody. (B) Arf-GTPase activities of nonphosphorylated (left panel) and phosphorylated ASAPl (right panel) are monitored in a fluorimetric Arfl-GTPase assay as a decrease of the intrinsic Arfl tryptophan fluorescence at 340 nm (in arbitrary units AU) upon excitation at 297.5 nm. Black dots indicate sample prior and grey dots after in vitro kinase reaction.

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. 

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