Role of the G protein gamma subunit in beta gamma complex modulation of phospholipase Cbeta function

The Journal of Biological Chemistry
Muslum AkgozN Gautam

Abstract

The G protein betagamma complex regulates a wide range of effectors, including the phospholipase C isozymes (PLCbetas). Different domains on the beta subunit are known to contact phospholipase Cbeta and affect its regulation. In contrast, the role of the gamma subunit in Gbetagamma modulation of PLCbeta function is not known. Results here show that the gamma subunit C-terminal domain is involved in mediating Gbetagamma interactions with phospholipase Cbeta. Mutations were introduced to alter the position of the post-translational prenyl modification at the C terminus of the gamma subunit with reference to the beta subunit. These mutants were appropriately post-translationally modified with the geranylgeranyl moiety. A deletion that shortened the C-terminal domain, insertions that extended this domain, and a point mutation, F59A, that disrupted the interaction of this domain with the beta subunit were all affected in their ability to activate PLCbeta to varying degrees. All mutants, however, interacted equally effectively with the G(o)alpha subunit. The results indicate that the G protein gamma subunit plays a direct role in the modulation of effector function by the betagamma complex.

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Citations

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Oct 11, 2003·Biochemical and Biophysical Research Communications·T Prescott AtkinsonPerry M Kirkham
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Aug 24, 2004·The Journal of Biological Chemistry·Kristi R KerchnerJames C Garrison
Nov 23, 2005·The Journal of Biological Chemistry·Linnia H MayeenuddinJames C Garrison
Dec 2, 2005·Molecular Pharmacology·Chang-Seon MyungJames C Garrison
Jul 25, 2013·Molecular Pharmacology·Angeline M Lyon, John J G Tesmer
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Mar 17, 2007·The Journal of Biological Chemistry·Denis J DupréTerence E Hébert
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