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Current work focuses on mechanisms of G protein activation by an intracellular guanine nucleotide exchange factor called Ric-8A. This protein appears to carry out multiple functions in cells: it is essential for asymmetric cell division and abscission, regulates neurotransmitter secretion and assists in the biogenesis of G protein alpha subunits, in addition to its role as a G protein activator. Ric-8A functions as a guanine nucleotide exchange factor by catalyzing the release of GDP from G alpha subunits. Ric-8A forms a nucleotide-free complex with G alpha, which dissociates only in the presence of GTP, leading to the formation of active GTP-bound alpha. In this regard, Ric-8A is functionally analogous to the well-characterized family of trans-membrane G Protein-Coupled Receptors (GPCR), which, upon agonist binding, catalyze nucleotide exchange from G protein heterotrimers.
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PROTEIN SCIENCE (2023)
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Daniel Munoz-Reyes,Levi J. Mcclelland, Sandra Arroyo-Urea,Sonia Sanchez-Yepes, Juan Sabin, Sara Perez-Suarez,Margarita Menendez,Alicia Mansilla,Javier Garcia-Nafria,Stephen Sprang,Maria Jose Sanchez-Barrena
ELIFE (2023)
biorxiv(2022)
Biophysical Journalno. 3 (2020): 335a
biorxiv(2020)
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