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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1991-12-26
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pubmed:databankReference |
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pubmed:abstractText |
We have conducted a genetic screen for mutations that decrease the effectiveness of signaling by a protein tyrosine kinase, the product of the Drosophila melanogaster sevenless gene. These mutations define seven genes whose wild-type products may be required for signaling by sevenless. Four of the seven genes also appear to be essential for signaling by a second protein tyrosine kinase, the product of the Ellipse gene. The putative products of two of these seven genes have been identified. One encodes a ras protein. The other locus encodes a protein that is homologous to the S. cerevisiae CDC25 protein, an activator of guanine nucleotide exchange by ras proteins. These results suggest that the stimulation of ras protein activity is a key element in the signaling by sevenless and Ellipse and that this stimulation may be achieved by activating the exchange of GTP for bound GDP by the ras protein.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins p21(ras),
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/ras Guanine Nucleotide Exchange...,
http://linkedlifedata.com/resource/pubmed/chemical/sev protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
67
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
701-16
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:1934068-Amino Acid Sequence,
pubmed-meshheading:1934068-DNA Mutational Analysis,
pubmed-meshheading:1934068-Drosophila Proteins,
pubmed-meshheading:1934068-Eye Proteins,
pubmed-meshheading:1934068-GTP-Binding Proteins,
pubmed-meshheading:1934068-Genes,
pubmed-meshheading:1934068-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:1934068-Membrane Glycoproteins,
pubmed-meshheading:1934068-Molecular Sequence Data,
pubmed-meshheading:1934068-Photoreceptor Cells,
pubmed-meshheading:1934068-Protein-Tyrosine Kinases,
pubmed-meshheading:1934068-Proteins,
pubmed-meshheading:1934068-Proto-Oncogene Proteins p21(ras),
pubmed-meshheading:1934068-Receptor Protein-Tyrosine Kinases,
pubmed-meshheading:1934068-Restriction Mapping,
pubmed-meshheading:1934068-Saccharomyces cerevisiae,
pubmed-meshheading:1934068-Schizosaccharomyces,
pubmed-meshheading:1934068-Sequence Alignment,
pubmed-meshheading:1934068-Signal Transduction,
pubmed-meshheading:1934068-Structure-Activity Relationship,
pubmed-meshheading:1934068-ras Guanine Nucleotide Exchange Factors
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pubmed:year |
1991
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pubmed:articleTitle |
Ras1 and a putative guanine nucleotide exchange factor perform crucial steps in signaling by the sevenless protein tyrosine kinase.
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pubmed:affiliation |
Howard Hughes Medical Institute, University of California, Berkeley 94720.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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