NDLI: Xenopus oocyte germinal-vesicle breakdown induced by [Val12]Ras is inhibited by a cytosol-localized Ras mutant.

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Xenopus oocyte germinal-vesicle breakdown induced by [Val12]Ras is inhibited by a cytosol-localized Ras mutant.

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Xenopus oocyte germinal-vesicle breakdown induced by [Val12]Ras is inhibited by a cytosol-localized Ras mutant.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sigal, I. S. Gibbs, J. B. Schofield, T. L. Scolnick, E. M. Schaber, M. D.
Description	Author Affiliation: Gibbs JB ( Department of Molecular Biology, Merck Sharp & Dohme Research Laboratories, West Point, PA 19486.);
Abstract	The GTPase-activating protein (GAP) has been postulated to function either as a negative regulator or as a possible target protein of Ras in mammalian cells and Xenopus oocytes. Ras must be localized in the plasma membrane of vertebrate cells to function, but GAP is localized in the cytosol. To test whether Ras function depends on a cytosolic factor such as GAP, we microinjected into Xenopus oocytes a form of Saccharomyces cerevisiae RAS1 ([Leu68]RAS1 terminated at residue 185, called [Leu68]RAS1(term.] that lacks the consensus membrane localization site, does not respond to GAP in a GTPase assay, but binds to GAP 100-fold more tightly than [Val12]Ras. [Leu68]RAS1(term.) alone did not stimulate oocyte germinal-vesicle breakdown. Instead, [Leu68]RAS1(term.) was observed to inhibit the action of insulin-like growth factor 1 or microinjected [Val12]Ras but not the action of progesterone as monitored by germinal-vesicle breakdown. Coinjection of purified mammalian GAP with [Leu68]RAS1(term.) reduced the inhibition of [Val12]Ras-stimulated germinal-vesicle breakdown. The results raise the possibility that a cytosolic factor is required for the action of [Val12]Ras in Xenopus oocytes and that this factor is either GAP or another protein with which GAP can compete for binding to [Leu68]RAS1(term.).
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Genes, Ras Membrane Proteins Metabolism Mutation Oocytes Physiology Proto-Oncogene Proteins Valine Animals Cells, Cultured Cytosol GTP Phosphohydrolases GTPase-Activating Proteins Mice Models, Theoretical Ultrastructure Proteins Genetics Proto-Oncogene Proteins P21(ras) Xenopus Laevis Ras GTPase-Activating Proteins Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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