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A more recent version of this article appeared on December 8, 2000
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C000604200v1
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Papers In Press, published online ahead of print October 19, 2000
J. Biol. Chem, 10.1074/jbc.C000604200
Submitted on September 1, 2000
Revised on October 2, 2000
Accepted on October 19, 2000

Selective role of G protein gamma subunits in receptor interaction

Yongmin Hou, Inaki Azpiazu, Alan Smrcka, and N. Gautam

Department of Anesthesiology, Washington University Medical School, St. Louis, MO 63110

Corresponding Author: gautam{at}morpheus.wustl.edu

Receptor stimulation of nucleotide exchange in a heterotrimeric G protein (alpha beta gamma ) is the primary event modulating signaling by G proteins. The molecular mechanisms at the basis of this event and the role of the G protein subunits, especially the beta gamma complex in receptor activation are unclear. In a reconstituted system, a purified muscarinic receptor, M2, activates G protein heterotrimers alpha i2beta 1gamma 5 and alpha i2beta 1gamma 7 with equal efficacy. However, when the alpha subunit type is substituted with alpha o, alpha obeta 1gamma 7 shows a 100% increase in M2 stimulated GTP hydrolysis compared to alpha obeta 1gamma 5. Using a sensitive assay based on betagamma complex stimulation of phospholipase C activity, we show that both beta 1gamma 5 and beta 1gamma 7 form heterotrimers equally well with alpha o and alpha i. These results indicate that the gamma subunit interaction with a receptor is critical for modulating nucleotide exchange and is influenced by the subunit type composition of the heterotrimer.


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