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A GDP Dissociation Inhibitor That Serves as a GTPase Inhibitor for the Ras-Like Protein CDC42Hs
Abstract
Members of the family of Ras-related guanosine triphosphate (GTP) binding proteins appear to take part in the regulation of a number of biological processes, including cell growth and differentiation. Three different classes of proteins that regulate the GTP binding and GTP hydrolytic activities of the Ras family members have been identified. These different regulatory proteins inhibit guanosine diphosphate (GDP) dissociation (designated as GDIs), stimulate GDP dissociation and GDP-GTP exchange (designated as GDSs), or stimulate GTP hydrolysis (designated as GAPs). In the case of the Ras-like protein CDC42Hs, which is the human homolog of a Saccharomyces cerevisiae cell division cycle protein, the GDI protein also inhibited both the intrinsic and GAP-stimulated hydrolysis of GTP. These findings establish an additional role for the GDI protein—namely, as a guanosine triphosphatase (GTPase) inhibitory protein for a Ras-like GTP binding protein.
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“Finally, Rho GDI𝛂 or Rho GDI-1 has also been shown to be capable of inhibiting GAP activity (22).”
From The Hematopoiesis-Specific GTP-Binding Protein RhoH Is GTPase Deficient and Modulates Activities of Other Rho GTPases by an Inhibitory Function (2002) · cites this paper as [22]
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Research works printed but not linked: 27
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Cited by
Cell Wall Integrity Signaling in Saccharomyces cerevisiae
Levin, D. E. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.2.262-291.2005 · Cited by 1,136
Li, X., Bu, X., Lu, B., Avraham, H., Flavell, R. A., & Lim, B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1158-1171.2002 · Cited by 153
Noh, H. J., Ponting, C. P., Boulding, H. C., Meader, S., Betancur, C., Buxbaum, J. D., Pinto, D., Marshall, C. R., Lionel, A. C., Scherer, S. W., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003523 · Cited by 54
Metadata
- Authors
- Hart, M. J., Maru, Y., Leonard, D., Witte, O. N., Evans, T., & Cerione, R. A.
- Affiliations
- Department of Biochemistry, Cell, and Molecular Biology, Cornell University, Ithaca, NY 14853.
- Department of Microbiology and Molecular Genetics and Molecular Biology Institute, Howard Hughes Medical Institute, University of California, Los Angeles, CA 90024.
- Department of Cell Biology, Genentech Inc., 460 Point San Bruno Boulevard, South San Francisco, CA 94080.
- Venue
- Science
- Published
- 1992-10-30
- Volume
- 258
- Issue
- 5083
- Pages
- 812-815
- ISSN
- 0036-8075
- 1095-9203
- Cited by
- 130
- References
- 0
- Language
- en
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