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Molecular & Cellular Proteomics 5:671-685, 2006.
© 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Proteomic Analysis of Bovine Brain G Protein Subunit Processing Heterogeneity^*,S

Lana A. Cook, Kevin L. Schey, Michael D. Wilcox, Jane Dingus, Rebecca Ettling, Troy Nelson, Daniel R. Knapp and John D. Hildebrandt

From the Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina 29425

We characterized the variable processing of the G protein subunit isoforms associated with bovine brain G proteins, a primary mediator of cellular communication. G subunits were isolated from purified brain G proteins and characterized by Edman sequencing, by MALDI MS, by chemical and/or enzymatic fragmentation assayed by MALDI MS, and by MS/MS fragmentation and sequencing. Multiple forms of six different G isoforms were detected. Significant variation in processing was found at both the amino termini and particularly the carboxyl termini of the proteins. All G isoforms contain a carboxyl-terminal CAAX motif for prenylation, carboxyl-terminal proteolysis, and carboxymethylation. Characterization of these proteins indicates significant variability in the normal processing of all of these steps in the prenylation reaction, including a new variation of prenyl processing resulting from cysteinylation of the carboxyl terminus. These results have multiple implications for intracellular signaling mechanisms by G proteins, for the role of prenyl processing variation in cell signaling, and for the site of action and consequences of drugs that target the prenylation modification.

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