Gem protein signaling and regulation.

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Gem protein signaling and regulation. Abstract Text:

Yvona Ward,Kathleen Kelly,

Gem is a member of the RGK family of GTP-binding proteins within the Ras superfamily possessing a ras-like core and terminal extensions. We have used a variety of cell-based assays to investigate the physiological role of Gem and combined these assays with site-directed mutagenesis of Gem protein to identify the sites responsible for regulation of Gem activity. One function of Gem that has been explained is the inhibition of Rho kinase (ROK)-mediated cytoskeletal rearrangement. Transient expression of Gem in endothelial cells and stable transfection of fibroblasts resulted in decreased stress fiber formation and focal adhesion assembly. A neurite extension model using N1E-115 murine neuroblastoma showed that Gem inhibits actinomyosin-related contractility by specifically opposing ROKbeta activity. Phospho-specific antibodies were used in Western blot analysis to show that Gem prevents phosphorylation of the regulatory subunit of myosin light chain and myosin phosphatase by ROKbeta. On the contrary, LIMK, another substrate of ROKbeta, was unaffected by Gem expression as demonstrated by an in vitro kinase assay, suggesting that Gem exerts its effect by changing the substrate specificity of ROKbeta rather than by blocking its catalytic activity. Point mutations of Gem at serines 261 and 289 in the carboxyl-terminus inhibited Gem function, indicating that posttranslational phosphorylation of these serines regulates Gem's effect on cytoskeletal reorganization. Another biological role of Gem is inhibition of voltage-gated calcium channel activity. By use of a PC12 cell model combined with site-directed mutagenesis, we demonstrated that Gem inhibits growth hormone secretion stimulated by calcium influx through L-type calcium channels and that this function is dependent on GTP and calmodulin binding to Gem. The theory and method for the assays discussed previously are reviewed here.

Gem protein signaling and regulation. Publishing Authors By Initials

Y Ward,K Kelly,

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Gem protein signaling and regulation. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Methods in enzymology

VOLUME: 407

Page Numbers: 468-83

Journal Abbreviation: Meth. Enzymol.

ISSN: 0076-6879

DAY: 7

MONTH: 06

YEAR: 2005

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LANGUAGE: eng

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Country: United States

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MEDLINETA: Methods Enzymol

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