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rdf:type |
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lifeskim:mentions |
umls-concept:C0002520,
umls-concept:C0036025,
umls-concept:C0041538,
umls-concept:C0143630,
umls-concept:C0205101,
umls-concept:C1167313,
umls-concept:C1314939,
umls-concept:C1366480,
umls-concept:C1704259,
umls-concept:C1705987,
umls-concept:C1710082,
umls-concept:C1879547
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pubmed:issue |
2-3
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pubmed:dateCreated |
2001-5-17
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pubmed:abstractText |
In response to external amino acids, the permease-like sensor Ssy1 of Saccharomyces cerevisiae activates a pathway leading to transcriptional induction of several permease genes including AGP1 and PTR2. We previously reported that AGP1 induction requires Grr1, the F-box protein part of the SCF(Grr1) ubiquitin-ligase complex. We show here that ubiquitin, other components of SCF(Grr1) and the ubiquitin-conjugating enzyme Cdc34 are essential for AGP1 and PTR2 induction. This suggests that transduction to these genes of the amino acid signal generated by Ssy1 involves an SCF(Grr1)-catalysed ubiquitination step.
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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/Amino Acid Transport Systems,
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/F-Box Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GRR1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PTR2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SSY1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/anaphase-promoting complex,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Galactosidase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
496
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
81-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11356187-Amino Acid Transport Systems,
pubmed-meshheading:11356187-Amino Acids,
pubmed-meshheading:11356187-Carrier Proteins,
pubmed-meshheading:11356187-Dose-Response Relationship, Drug,
pubmed-meshheading:11356187-F-Box Proteins,
pubmed-meshheading:11356187-Fungal Proteins,
pubmed-meshheading:11356187-Gene Deletion,
pubmed-meshheading:11356187-Genotype,
pubmed-meshheading:11356187-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:11356187-Ligases,
pubmed-meshheading:11356187-Membrane Proteins,
pubmed-meshheading:11356187-Membrane Transport Proteins,
pubmed-meshheading:11356187-Saccharomyces cerevisiae,
pubmed-meshheading:11356187-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11356187-Signal Transduction,
pubmed-meshheading:11356187-Time Factors,
pubmed-meshheading:11356187-Transcription, Genetic,
pubmed-meshheading:11356187-Transduction, Genetic,
pubmed-meshheading:11356187-Ubiquitin-Protein Ligase Complexes,
pubmed-meshheading:11356187-Ubiquitin-Protein Ligases,
pubmed-meshheading:11356187-Ubiquitins,
pubmed-meshheading:11356187-beta-Galactosidase
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pubmed:year |
2001
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pubmed:articleTitle |
Ubiquitin and the SCF(Grr1) ubiquitin ligase complex are involved in the signalling pathway activated by external amino acids in Saccharomyces cerevisiae.
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pubmed:affiliation |
Laboratoire de Physiologie Cellulaire, Université Libre de Bruxelles CP 300, Institut de Biologie et de Médecine Moléculaires, rue des Pr. Jeener et Brachet 10, 6041, Gosselies, Belgium.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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