Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-4-23
pubmed:abstractText
Cyclin C belongs to the cyclin family of proteins that control cell cycle transitions through activation of specific catalytic subunits, the cyclin-dependent kinases (CDKs). However, there is as yet no evidence for any role of cyclin C and its partner, cdk8, in cell cycle regulation. Rather, the cyclin C-cdk8 complex was found associated with the RNA polymerase II transcription machinery. The periodic degradation of bona fide cyclins is crucial for cell-cycle progression and depends on the catalytic activity of the associated CDK. Here we show that endogenous cyclin C protein is quite stable with a half-life of 4 h. In contrast, exogenously expressed cyclin C is very unstable (half-life 15 min) and degraded by the ubiquitin-proteasome pathway. Co-expression with its associated cdk, however, strongly stabilizes cyclin C and results in a protein half-life near that of endogenous cyclin C. In stark contrast to data reported for other members of the cyclin family, both catalytically active and inactive cdk8 induce cyclin C stabilization. Moreover, this stabilization is accompanied in both cases by phosphorylation of the cyclin, which is not detectable when unstable. Our results indicate that cyclin C has apparently diverged from other cyclins in the regulation of its stability by its CDK partner.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/CCNC protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CDK8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Ccnc protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin C, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinase 8, http://linkedlifedata.com/resource/pubmed/chemical/Cyclin-Dependent Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
551-62
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11313987-3T3 Cells, pubmed-meshheading:11313987-Animals, pubmed-meshheading:11313987-COS Cells, pubmed-meshheading:11313987-Catalysis, pubmed-meshheading:11313987-Cyclin C, pubmed-meshheading:11313987-Cyclin-Dependent Kinase 8, pubmed-meshheading:11313987-Cyclin-Dependent Kinases, pubmed-meshheading:11313987-Cyclins, pubmed-meshheading:11313987-Cysteine Endopeptidases, pubmed-meshheading:11313987-Drug Stability, pubmed-meshheading:11313987-Gene Expression Regulation, pubmed-meshheading:11313987-Half-Life, pubmed-meshheading:11313987-HeLa Cells, pubmed-meshheading:11313987-Humans, pubmed-meshheading:11313987-Mice, pubmed-meshheading:11313987-Multienzyme Complexes, pubmed-meshheading:11313987-Phosphorylation, pubmed-meshheading:11313987-Proteasome Endopeptidase Complex, pubmed-meshheading:11313987-Protein-Serine-Threonine Kinases, pubmed-meshheading:11313987-Ubiquitins
pubmed:year
2001
pubmed:articleTitle
Human cyclin C protein is stabilized by its associated kinase cdk8, independently of its catalytic activity.
pubmed:affiliation
Institut de Genetique Moleculaire de Montpellier, CNRS UMR 5535, IFR24, 1919, route de Mende, 34293 Montpellier Cedex 5, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't