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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1996-8-23
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pubmed:abstractText |
The alpha-factor pheromone receptor stimulates MATa yeast cells to undergo conjugation. The receptor contains seven transmembrane domains that function in ligand binding and in transducing a signal to the cytoplasmic receptor sequences to mediate G protein activation. A genetic screen was used to isolate receptor mutations that constitutively signal in the absence of alpha-factor. The Pro-258-->Leu (P258L) mutation caused constitutive receptor signaling that was equivalent to about 45% of the maximum level observed in wild-type cells stimulated with alpha-factor. Mutations of both Pro-258 and the adjacent Ser-259 to Leu increased constitutive signaling to > or = 90% of the maximum level. Since Pro-258 occurs in the central portion of transmembrane domain 6, and since proline residues are expected to cause a kink in alpha-helical domains, the P258L mutation is predicted to alter the structure of transmembrane domain 6. The P258L mutation did not result in a global distortion of receptor structure because alpha-factor bound to the mutant receptors with high affinity and induced even higher levels of signaling. These results suggest that sequences surrounding Pro-258 may be involved in ligand activation of the receptor. Conformational changes in transmembrane domain 6 may effect a change in the adjacent sequences in the third intracellular loop that are thought to function in G protein activation. Greater than 90% of all G protein-coupled receptors contain a proline residue at a similar position in transmembrane domain 6, suggesting that this aspect of receptor activation may be conserved in other receptors.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1323233,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1324410,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1346134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1356370,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1455506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-16453635,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1652922,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1657404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-1848192,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-2005794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-2016741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-2017168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-2147873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-2161538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-2842059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-2844413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-3001640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-3023832,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-3073106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-3302672,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-6287580,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-6358212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-6360378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-6993497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-7622478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-7692306,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-7701349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-7823940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-7834739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-7935439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8095116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8095262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8132618,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8164685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8234336,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8249148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8288649,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8385611,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8392878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8393865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8413281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8413622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8413627,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8458079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8464048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8692892-8524302
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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/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Pheromones,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Mating Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/mating factor
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
93
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6764-9
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:8692892-Amino Acid Sequence,
pubmed-meshheading:8692892-Cell Division,
pubmed-meshheading:8692892-GTP-Binding Proteins,
pubmed-meshheading:8692892-Genes, Dominant,
pubmed-meshheading:8692892-Membrane Proteins,
pubmed-meshheading:8692892-Molecular Sequence Data,
pubmed-meshheading:8692892-Morphogenesis,
pubmed-meshheading:8692892-Mutagenesis,
pubmed-meshheading:8692892-Mutation,
pubmed-meshheading:8692892-Peptides,
pubmed-meshheading:8692892-Pheromones,
pubmed-meshheading:8692892-Proline,
pubmed-meshheading:8692892-Protein Binding,
pubmed-meshheading:8692892-Receptors, Mating Factor,
pubmed-meshheading:8692892-Receptors, Peptide,
pubmed-meshheading:8692892-Saccharomyces cerevisiae,
pubmed-meshheading:8692892-Signal Transduction,
pubmed-meshheading:8692892-Transcription Factors
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pubmed:year |
1996
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pubmed:articleTitle |
Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled alpha-factor receptor.
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