Document Detail


Properties of the SDC25 C-domain, a GDP to GTP exchange factor of RAS proteins and in vitro modulation of adenylyl cyclase.
MedLine Citation:
PMID:  8325863     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The SDC25 C-domain, the product encoded by the 3'-terminal part of the Saccharomyces cerevisiae SDC25 gene, acts as a GDP dissociation stimulator on RAS proteins (Créchet, J.B., Poullet, P., Mistou, M. Y., Parmeggiani, A., Camonis, J., Boy-Marcotte, E., Damak, F., and Jacquet, M. (1990b) Science 248, 866-868). To define further its role in the RAS-adenylyl cyclase pathway, an in vitro system was used, which utilized cell membranes from yeast strains with appropriate genotypes carrying alterations in the positive regulators of adenylyl cyclase activity. The SDC25 C-domain was able to stimulate the adenylyl cyclase activity of membranes from RAS2 cdc25 strains. Our results indicate that the SDC25 C-domain activates adenylyl cyclase by rapidly recycling the active RAS2. or RAS1.GTP complex from the respective GDP complex. This is also supported by the observation that the stimulation of adenylyl cyclase activity by RAS2T152I, a mutant characterized by a constitutively fast GDP to GTP exchange, was insensitive to the action of the SDC25 C-domain. No direct influence of this GDP dissociation stimulator on adenylyl cyclase was detected. Biochemical evidence was obtained, showing that in the presence of the functional target of RAS, the adenylyl cyclase, the effects of SDC25 C-domain and the catalytic domain of GTPase-activating protein are antagonistic. This in vitro system allowed a quantitative evaluation of the effects of positive and negative effectors of RAS on adenylyl cyclase and the biochemical analysis of conditions inducing a phenotype of permanently activated adenylyl cyclase.
Authors:
J B Créchet; P Poullet; A Bernardi; O Fasano; A Parmeggiani
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  268     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1993 Jul 
Date Detail:
Created Date:  1993-08-12     Completed Date:  1993-08-12     Revised Date:  2009-07-22    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  14836-41     Citation Subset:  IM    
Affiliation:
S.D.I. 61840 du Centre National de la Recherche Scientifique, Laboratoire de Biochimie, Ecole Polytechnique, Palaiseau, France.
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MeSH Terms
Descriptor/Qualifier:
Adenylate Cyclase / metabolism*
Enzyme Activation
Fungal Proteins / chemistry,  genetics,  metabolism*
GTP-Binding Proteins / genetics*,  metabolism
Genotype
Saccharomyces cerevisiae / enzymology,  genetics,  metabolism*
Saccharomyces cerevisiae Proteins*
rap GTP-Binding Proteins
ras Proteins*
Chemical
Reg. No./Substance:
0/Fungal Proteins; 0/Saccharomyces cerevisiae Proteins; EC 3.6.1.-/GTP-Binding Proteins; EC 3.6.5.2/RAS1 protein, S cerevisiae; EC 3.6.5.2/RAS2 protein, S cerevisiae; EC 3.6.5.2/rap GTP-Binding Proteins; EC 3.6.5.2/ras Proteins; EC 4.6.1.1/Adenylate Cyclase

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