|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
6
|
|
pubmed:dateCreated |
2002-12-30
|
|
pubmed:abstractText |
Cullin proteins assemble a large number of RING E3 ubiquitin ligases and regulate various physiological processes. Covalent modification of cullins by the ubiquitin-like protein NEDD8 activates cullin ligases through an as yet undefined mechanism. We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a ternary complex with CUL1 and ROC1. CAND1 dissociated SKP1 from CUL1 and inhibited SCF ligase activity in vitro. Suppression of CAND1 in vivo increased the level of the CUL1-SKP1 complex. We suggest that by restricting SKP1-CUL1 interaction, CAND1 regulated the assembly of productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to be utilized by a large number of SKP1-F box-substrate subcomplexes.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CAND1 protein, human,
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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/F-Box Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/NEDD8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Synthases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SKP Cullin F-Box Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/SKP1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Dec
|
|
pubmed:issn |
1097-2765
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
10
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1511-8
|
|
pubmed:dateRevised |
2010-6-2
|
|
pubmed:meshHeading |
pubmed-meshheading:12504025-Amino Acid Sequence,
pubmed-meshheading:12504025-Bacterial Proteins,
pubmed-meshheading:12504025-Carrier Proteins,
pubmed-meshheading:12504025-Cell Cycle Proteins,
pubmed-meshheading:12504025-Cullin Proteins,
pubmed-meshheading:12504025-DNA-Binding Proteins,
pubmed-meshheading:12504025-Enzyme Inhibitors,
pubmed-meshheading:12504025-F-Box Proteins,
pubmed-meshheading:12504025-Genes, myc,
pubmed-meshheading:12504025-Humans,
pubmed-meshheading:12504025-Kinetics,
pubmed-meshheading:12504025-Ligases,
pubmed-meshheading:12504025-Macromolecular Substances,
pubmed-meshheading:12504025-Molecular Sequence Data,
pubmed-meshheading:12504025-Mutagenesis, Site-Directed,
pubmed-meshheading:12504025-Peptide Synthases,
pubmed-meshheading:12504025-Recombinant Proteins,
pubmed-meshheading:12504025-SKP Cullin F-Box Protein Ligases,
pubmed-meshheading:12504025-Saccharomyces cerevisiae,
pubmed-meshheading:12504025-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12504025-Transcription Factors,
pubmed-meshheading:12504025-Ubiquitins
|
|
pubmed:year |
2002
|
|
pubmed:articleTitle |
NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.
|
|
pubmed:affiliation |
Department of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center, Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
