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Papers In Press, published online ahead of print September 6, 2001
Department of Anesthesiology, Washington University Medical School, St. Louis, MO 63110
Corresponding Author: gautam{at}morpheus.wustl.edu
The surfaces of heterotrimeric G proteins (alpha-beta-gamma) in contact with receptors and the molecular events at these sites which lead to G protein activation are largely unknown. We show here that a peptide from the C terminus of a G protein gamma subunit blocks muscarinic receptor stimulated G protein activation in a sequence dependent fashion. A G protein mutated at the same site on the gamma subunit shows enhanced receptor stimulated nucleotide exchange without affecting G protein heterotrimerization. Ineffective contact between the gamma subunit and receptor increases the rate of receptor stimulated nucleotide exchange. Specific interaction of the G protein gamma subunit with the receptor thus helps the betagamma complex to act at a distance and control guanine nucleotide exchange in the alpha subunit.
J. Biol. Chem, 10.1074/jbc.M104034200
Submitted on May 4, 2001
Revised on September 6, 2001
Accepted on September 6, 2001
G protein gamma subunit interaction with a receptor regulates receptor stimulated nucleotide exchange
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