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Submitted on July 18, 2005
Accepted on December 5, 2005

Proteomic analysis of bovine brain G protein gamma subunit processing heterogeneity

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

Pharmacology Dept., Medical University of South Carolina, Charleston, SC 29425

Corresponding Author: hildebjd{at}musc.edu

We have characterized the variable processing of the G protein gamma subunit isoforms associated with bovine brain G proteins, a primary mediator of cellular communication. Ggamma subunits were isolated from purified brain G proteins and characterized by Edman sequencing, by MALDI mass spectrometry (MS), by chemical and/or enzymatic fragmentation assayed by MALDI MS and by MS/MS fragmentation and sequencing. Multiple forms of 6 different Ggamma isoforms were detected. Significant variation in processing was found at both the N-termini and, particularly, the C-termini of the proteins. All Ggamma isoforms contain a C-terminal CaaX motif for prenylation, C-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 C-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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