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M107661200v1
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Papers In Press, published online ahead of print September 6, 2001
J. Biol. Chem, 10.1074/jbc.M107661200
Submitted on August 10, 2001
Revised on September 6, 2001
Accepted on September 6, 2001

Role of the gamma subunit prenyl moiety in G-protein {betagamma} complex interaction with phospholipase C-beta

Vanessa Chang Fogg, Inaki Azpiazu, Maurine E. Linder, Alan Smrcka, Suzanne Scarlata, and N. Gautam

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

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

The G protein betagamma complex regulates a wide range of effectors, including the phospholipase C-beta isozymes (PLC-betas). Prenyl modification of the gamma subunit is necessary for this activity. Evidence presented here supports a direct interaction between the G-protein gamma subunit prenyl group and PLC-beta isozymes. A geranylgeranylated peptide corresponding to the C-terminal region of the gamma subunit type, gamma2, strongly inhibits stimulation of PLC-beta2 and PLC-beta3 activity by the betagamma complex. This effect is specific because the same peptide has no effect on stimulation of PLC-beta by an alpha subunit type, alphaq. Prenylation of the gamma peptide is required for its inhibitory effect. When interaction of prenylated gamma subunit peptide to fluorophore tagged PLC-beta2 was examined by fluorescence spectroscopy, prenylated but not unprenylated peptide increased PLC-beta2 fluorescence emission energy indicating direct binding of the prenyl moiety to PLC-beta. In addition, fluorescence resonance energy transfer (FRET) was detected between fluorophore tagged PLC-beta and wild type betagamma complex but not an unprenylated mutant betagamma complex. We conclude that a major function of the gamma subunit prenyl group is to facilitate direct protein-protein interaction between the betagamma complex and an effector, phospholipase C-beta.


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