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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6955
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pubmed:dateCreated |
2003-9-18
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pubmed:abstractText |
Programmed destruction of regulatory proteins through the ubiquitin-proteasome system is a widely used mechanism for controlling signalling pathways. Cullins are proteins that function as scaffolds for modular ubiquitin ligases typified by the SCF (Skp1-Cul1-F-box) complex. The substrate selectivity of these E3 ligases is dictated by a specificity module that binds cullins. In the SCF complex, this module is composed of Skp1, which binds directly to Cul1, and a member of the F-box family of proteins. F-box proteins bind Skp1 through the F-box motif, and substrates by means of carboxy-terminal protein interaction domains. Similarly, Cul2 and Cul5 interact with BC-box-containing specificity factors through the Skp1-like protein elongin C. Cul3 is required for embryonic development in mammals and Caenorhabditis elegans but its specificity module is unknown. Here we report the identification of a large family of BTB-domain proteins as substrate-specific adaptors for C. elegans CUL-3. Biochemical studies using the BTB protein MEL-26 and its genetic target MEI-1 (refs 12, 13) indicate that BTB proteins merge the functional properties of Skp1 and F-box proteins into a single polypeptide.
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pubmed:grant |
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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/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/CUL3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Cullin Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MEI-1 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/MEI-2 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Mel-26 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/SKP Cullin F-Box Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1476-4687
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
425
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
316-21
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pubmed:dateRevised |
2010-12-17
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pubmed:meshHeading |
pubmed-meshheading:13679922-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:13679922-Adenosine Triphosphatases,
pubmed-meshheading:13679922-Amino Acid Motifs,
pubmed-meshheading:13679922-Amino Acid Sequence,
pubmed-meshheading:13679922-Animals,
pubmed-meshheading:13679922-Caenorhabditis elegans,
pubmed-meshheading:13679922-Caenorhabditis elegans Proteins,
pubmed-meshheading:13679922-Carrier Proteins,
pubmed-meshheading:13679922-Cell Cycle Proteins,
pubmed-meshheading:13679922-Cell Line,
pubmed-meshheading:13679922-Cullin Proteins,
pubmed-meshheading:13679922-Humans,
pubmed-meshheading:13679922-Models, Molecular,
pubmed-meshheading:13679922-Molecular Sequence Data,
pubmed-meshheading:13679922-Mutation,
pubmed-meshheading:13679922-Peptide Synthases,
pubmed-meshheading:13679922-Protein Binding,
pubmed-meshheading:13679922-Protein Structure, Tertiary,
pubmed-meshheading:13679922-SKP Cullin F-Box Protein Ligases,
pubmed-meshheading:13679922-Substrate Specificity,
pubmed-meshheading:13679922-Two-Hybrid System Techniques
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pubmed:year |
2003
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pubmed:articleTitle |
BTB proteins are substrate-specific adaptors in an SCF-like modular ubiquitin ligase containing CUL-3.
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pubmed:affiliation |
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, Texas 77030, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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