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Originally published In Press as doi:10.1074/jbc.M101784200 on September 13, 2001

J. Biol. Chem., Vol. 276, Issue 48, 45153-45159, November 30, 2001
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The Role of Electrostatic Interactions in the Regulation of the Membrane Association of G Protein beta gamma Heterodimers*

Diana MurrayDagger §, Stuart McLaughlin||, and Barry HonigDagger **

From the Dagger  Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, New York, New York 10032 and the  Department of Physiology and Biophysics, State University of New York, Stony Brook, New York 11794-8661

In this paper we report calculations of electrostatic interactions between the transducin (Gt) beta gamma heterodimer (Gtbeta gamma ) and phospholipid membranes. Although membrane association of Gtbeta gamma is due primarily to the hydrophobic penetration into the membrane interior of a farnesyl chain attached to the gamma  subunit, structural studies have revealed that there is a prominent patch of basic residues on the surface of the beta  subunit surrounding the site of farnesylation that is exposed upon dissociation from the Gtalpha subunit. Moreover, phosducin, which produces dissociation of Gtbeta gamma from membranes, interacts directly with Gtbeta gamma and introduces a cluster of acidic residues into this region. The calculations, which are based on the finite difference Poisson-Boltzmann method, account for a number of experimental observations and suggest that charged residues play a role in mediating protein-membrane interactions. Specifically, the calculations predict the following. 1) Favorable electrostatic interactions enhance the membrane partitioning due to the farnesyl group by an order of magnitude although Gtbeta gamma has a large net negative charge (-12). 2) This electrostatic attraction positions Gtbeta gamma so that residues implicated in mediating the interaction of Gtbeta gamma with its membrane-bound effectors are close to the membrane surface. 3) The binding of phosducin to Gtbeta gamma diminishes the membrane partitioning of Gtbeta gamma by an order of magnitude. 4) Lowering the ionic strength of the solution converts the electrostatic attraction into a repulsion. Sequence analysis and homology model building suggest that our conclusions may be generalized to other Gbeta gamma and phosducin isoforms as well.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a Helen Hay Whitney Foundation postdoctoral fellowship and a United States Department of Energy/Sloan Foundation Postdoctoral Fellowship in Computational Molecular Biology. Present address: Dept. of Microbiology and Immunology, Weill Cornell Medical School, 1300 York Ave., Box 62, New York, NY 10021.

|| Supported by National Institutes of Health Grant GM24971 and National Science Foundation Grant MCB9729538.

** Supported by National Science Foundation Grant MCB-9808902 and received supercomputing support from National Center for Supercomputing Applications (NSCA) Grant MCA95C015 and the Frederick Biomedical Supercomputing Center (FBSC). To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, 630 West 168th St., New York, NY 10032. Tel.: 212-305-7970; Fax: 212-305-6926; E-mail: bh6@columbia.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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