Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1-2
|
| pubmed:dateCreated |
1995-2-22
|
| pubmed:abstractText |
Ras proteins bound to GDP are biologically inactive while those bound to GTP are active. Ras-specific guanine nucleotide-exchange factors (GEFs) have been shown to activate Ras proteins. We used oligodeoxyribonucleotide primers with sequences similar to the cDNAs of rat and mouse cdc25 (encoding a Ras-GEF) to amplify, by the PCR, sequences with the potential to encode a 1275-amino-acid protein homologous to the rodent Cdc25GEF proteins. Northern blot analysis detected a brain-specific 5-kb transcript. We provide evidence for a novel alternately spliced transcript of cdc25 and show that these alternately spliced transcripts are differentially expressed in various regions of the adult nervous system. Antibodies raised against the C terminus of the protein recognize a 140-kDa protein in brain extracts of human, rat, guinea pig and cow; the 140-kDa protein is associated predominantly, if not exclusively, with a crude membrane fraction of brain. The C terminus of human Cdc25GEF can complement the loss of CDC25 function in Saccharomyces cerevisiae. A glutathione S-transferase fusion protein containing the C terminus of the cdc25 product can stimulate guanine nucleotide exchange on H-Ras in vitro. Further, the Cdc25-fusion protein binds tightly to the nucleotide-free form of H-Ras in vitro, and this binding is reversed by the addition of GTP.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras-GRF1
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0378-1119
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
30
|
| pubmed:volume |
151
|
| pubmed:geneSymbol |
cdc25,
cdc25<up>GEF</up>
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
279-84
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:7828890-Alternative Splicing,
pubmed-meshheading:7828890-Amino Acid Sequence,
pubmed-meshheading:7828890-Animals,
pubmed-meshheading:7828890-Binding Sites,
pubmed-meshheading:7828890-Brain,
pubmed-meshheading:7828890-Cattle,
pubmed-meshheading:7828890-Cloning, Molecular,
pubmed-meshheading:7828890-DNA, Complementary,
pubmed-meshheading:7828890-Guanosine Diphosphate,
pubmed-meshheading:7828890-Guanosine Triphosphate,
pubmed-meshheading:7828890-Guinea Pigs,
pubmed-meshheading:7828890-Hominidae,
pubmed-meshheading:7828890-Humans,
pubmed-meshheading:7828890-Kinetics,
pubmed-meshheading:7828890-Mice,
pubmed-meshheading:7828890-Molecular Sequence Data,
pubmed-meshheading:7828890-Phosphoprotein Phosphatases,
pubmed-meshheading:7828890-Plasmids,
pubmed-meshheading:7828890-Protein Biosynthesis,
pubmed-meshheading:7828890-Proteins,
pubmed-meshheading:7828890-Rats,
pubmed-meshheading:7828890-Transcription, Genetic,
pubmed-meshheading:7828890-ras Proteins,
pubmed-meshheading:7828890-ras-GRF1
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Cloning and analysis of human cDNAs encoding a 140-kDa brain guanine nucleotide-exchange factor, Cdc25GEF, which regulates the function of Ras.
|
| pubmed:affiliation |
Department of Biochemistry and Molecular Biology, USC/Norris Comprehensive Cancer Center, University of Southern California School of Medicine, Los Angeles 90033.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|