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A GDP Dissociation Inhibitor That Serves as a GTPase Inhibitor for the Ras-Like Protein CDC42Hs

1992; American Association for the Advancement of Science; Volume: 258; Issue: 5083 Linguagem: Inglês

10.1126/science.1439791

1095-9203

Matthew J. Hart, Yoshiro Maru, David A. Leonard, Owen N. Witte, Tony Evans, Richard A. Cerione,

Cellular transport and secretion

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.