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J. Biol. Chem., Vol. 276, Issue 45, 41797-41802, November 9, 2001

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Role of the  Subunit Prenyl Moiety in G Protein Complex Interaction with Phospholipase C^*

Vanessa C. Fogg, Inaki Azpiazu, Maurine E. Linder^§, Alan Smrcka^¶, Suzanne Scarlata, and N. Gautam^**

From the Departments of  Anesthesiology, ^** Genetics, and ^§ Cell Biology & Physiology, Washington University School of Medicine, St. Louis, Missouri 63110, the  Departments of Physiology & Biophysics and Molecular Genetics & Microbiology, State University of New York, Stony Brook, New York 11794, and the ^¶ Department of Pharmacology & Physiology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642

The G protein complex regulates a wide range of effectors, including the phospholipase C isozymes (PLCs). Prenyl modification of the  subunit is necessary for this activity. Evidence presented here supports a direct interaction between the G protein  subunit prenyl group and PLC isozymes. A geranylgeranylated peptide corresponding to the C-terminal region of the  subunit type, 2, strongly inhibits stimulation of PLC2 and PLC3 activity by the complex. This effect is specific because the same peptide has no effect on stimulation of PLC by an  subunit type, q. Prenylation of the  peptide is required for its inhibitory effect. When interaction of prenylated  subunit peptide to fluorophore-tagged PLC2 was examined by fluorescence spectroscopy, prenylated but not unprenylated peptide increased PLC2 fluorescence emission energy, indicating direct binding of the prenyl moiety to PLC. In addition, fluorescence resonance energy transfer was detected between fluorophore tagged PLC and wild type complex but not an unprenylated mutant complex. We conclude that a major function of the  subunit prenyl group is to facilitate direct protein-protein interaction between the complex and an effector, phospholipase C.

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