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J. Biol. Chem., Vol. 275, Issue 50, 38961-38964, December 15, 2000

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ACCELERATED PUBLICATION
Selective Role of G Protein  Subunits in Receptor Interaction^*

Yongmin Hou, Inaki Azpiazu, Alan Smrcka^§, and N. Gautam^¶

From the  Departments of Anesthesiology and ^¶ Genetics, Washington University School of Medicine, St. Louis, Missouri 63110 and the ^§ Department of Pharmacology and Physiology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642

Receptor stimulation of nucleotide exchange in a heterotrimeric G protein () 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 complex, in receptor activation are unclear. In a reconstituted system, a purified muscarinic receptor, M2, activates G protein heterotrimers i215 and i217 with equal efficacy. However, when the  subunit type is substituted with o, o17 shows a 100% increase in M2-stimulated GTP hydrolysis compared with o15. Using a sensitive assay based on complex stimulation of phospholipase C activity, we show that both 15 and 17 form heterotrimers equally well with o and i. These results indicate that the  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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