Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
beta2-Adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein.
- R. Premont, A. Claing, R. Lefkowitz
- Biology, Computer ScienceProceedings of the National Academy of Sciences…
- 24 November 1998
An essential role for ARF proteins in regulating beta2-adrenergic receptor endocytosis is suggested through regulation of ARF protein activation by GRK-mediated recruitment of the GIT1 ARF GAP to the plasma membrane.
Molecules in the ARF Orbit*
Criteria for designation as an ARF have been the ability to activate cholera toxin and to rescue mutant Saccharomyces cerevisiae bearing the lethal double deletion of ARF1 and ARF2 genes.
GIT Proteins, A Novel Family of Phosphatidylinositol 3,4,5-Trisphosphate-stimulated GTPase-activating Proteins for ARF6*
- N. Vitale, W. Patton, J. Moss, M. Vaughan, R. Lefkowitz, R. Premont
- Biology, Computer ScienceThe Journal of Biological Chemistry
- 5 May 2000
The results suggest that although the mechanism of GTP hydrolysis is probably very similar in these two families of ARF GAPs, GIT proteins might specifically regulate the activity of ARf6 in cells in coordination with phosphatidylinositol 3-kinase signaling pathways.
HORMONE-SENSITIVE LIPASE AND MONOGLYCERIDE LIPASE ACTIVITIES IN ADIPOSE TISSUE.
Structure and Function of ARF Proteins: Activators of Cholera Toxin and Critical Components of Intracellular Vesicular Transport Processes (*)
Molecular identification of ADP-ribosylation factor mRNAs and their expression in mammalian cells.
Characterization of an ADP-ribosylation Factor-like 1 Protein inSaccharomyces cerevisiae *
Biochemical analyses of purified recombinant yeast ARL1 (yARL1) protein revealed properties similar to those ARF and ARL2 proteins, including the ability to bind and hydrolyze GTP, and it may offer an opportunity to define an ARL function in another kind of vesicular trafficking, such as the regulated secretory pathway.
Purification and Cloning of a Brefeldin A-inhibited Guanine Nucleotide-exchange Protein for ADP-ribosylation Factors*
- Akira Togawa, N. Morinaga, M. Ogasawara, J. Moss, M. Vaughan
- BiologyThe Journal of Biological Chemistry
- 30 April 1999
Two new clones for the ∼200-kDa BIG1 and BIG2 should facilitate characterization of this rather different family of proteins as well as the elucidation of mechanisms of regulation of BFA-sensitive ARF function in Golgi transport.
Activation of rat brain phospholipase D by ADP-ribosylation factors 1,5, and 6: separation of ADP-ribosylation factor-dependent and oleate-dependent enzymes.
- D. Massenburg, J. Han, M. Vaughan
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 22 November 1994
The effects of recombinant ARF proteins from the three classes on cholera toxin activity did not correlate with those on PLD, consistent with the notion that different aspects of ARF structure are involved in the two functions.
Adp-Ribosylating Toxins and G Proteins: Insights into Signal Transduction
Bacterial ADP-ribosyltransferases: toxins and related proteins Guanine nucleotide-binding proteins coupled to signal transduction in animal cells ADP ribosylation in bacteria and animal cells