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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5414
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pubmed:dateCreated |
1999-5-11
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pubmed:abstractText |
Control of cyclin levels is critical for proper cell cycle regulation. In yeast, the stability of the G1 cyclin Cln1 is controlled by phosphorylation-dependent ubiquitination. Here it is shown that this reaction can be reconstituted in vitro with an SCF E3 ubiquitin ligase complex. Phosphorylated Cln1 was ubiquitinated by SCF (Skp1-Cdc53-F-box protein) complexes containing the F-box protein Grr1, Rbx1, and the E2 Cdc34. Rbx1 promotes association of Cdc34 with Cdc53 and stimulates Cdc34 auto-ubiquitination in the context of Cdc53 or SCF complexes. Rbx1, which is also a component of the von Hippel-Lindau tumor suppressor complex, may define a previously unrecognized class of E3-associated proteins.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/CLN1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cdc53 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclins,
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/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/S-Phase Kinase-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SKP Cullin F-Box Protein Ligases,
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
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
662-5
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pubmed:dateRevised |
2009-7-28
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pubmed:meshHeading |
pubmed-meshheading:10213692-Amino Acid Sequence,
pubmed-meshheading:10213692-Animals,
pubmed-meshheading:10213692-Carrier Proteins,
pubmed-meshheading:10213692-Cell Cycle Proteins,
pubmed-meshheading:10213692-Cell Line,
pubmed-meshheading:10213692-Cullin Proteins,
pubmed-meshheading:10213692-Cyclins,
pubmed-meshheading:10213692-F-Box Proteins,
pubmed-meshheading:10213692-Fungal Proteins,
pubmed-meshheading:10213692-Ligases,
pubmed-meshheading:10213692-Molecular Sequence Data,
pubmed-meshheading:10213692-Peptide Synthases,
pubmed-meshheading:10213692-Phosphorylation,
pubmed-meshheading:10213692-Recombinant Fusion Proteins,
pubmed-meshheading:10213692-S-Phase Kinase-Associated Proteins,
pubmed-meshheading:10213692-SKP Cullin F-Box Protein Ligases,
pubmed-meshheading:10213692-Saccharomyces cerevisiae,
pubmed-meshheading:10213692-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10213692-Sequence Alignment,
pubmed-meshheading:10213692-Ubiquitin-Protein Ligase Complexes,
pubmed-meshheading:10213692-Ubiquitin-Protein Ligases,
pubmed-meshheading:10213692-Ubiquitins
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pubmed:year |
1999
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pubmed:articleTitle |
Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1.
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pubmed:affiliation |
Verna and Marrs McLean Department of Biochemistry, Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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