Human cyclin C protein is stabilized by its associated kinase cdk8, independently of its catalytic activity

Barette, Caroline; Jariel-Encontre, Isabelle; Piechaczyk, Marc; Piette, Jacques

doi:10.1038/sj.onc.1204129

Cited by 53Cancer-related Molecular PathwaysUbiquitin and proteasome pathwaysMicrotubule and mitosis dynamics

Human cyclin C protein is stabilized by its associated kinase cdk8, independently of its catalytic activity

Barette, Caroline, Jariel-Encontre, Isabelle, Piechaczyk, Marc, Piette, Jacques·2001·Oncogene

DOI 10.1038/sj.onc.1204129

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Abstract

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.

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Authors: Barette, C., Jariel-Encontre, I., Piechaczyk, M., & Piette, J.
Affiliations: Centre National de la Recherche Scientifique (FR)
ORCID: Barette, Caroline
Piechaczyk, Marc
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2001-02-01
Volume: 20
Issue: 5
Pages: 551-562
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1204129
OpenAlex: W2326503995
Cited by: 52
References: 52
Citations by year: 2026: 1 · 2025: 6 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 3 · 2020: 2 · 2019: 2 · 2017: 1 · 2016: 1 · 2015: 1 · 2013: 5 · 2012: 3
FWCI: 1.03
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Keywords: cyclin C, CDK8, cyclin-dependent kinases, protein stability, protein half-life, ubiquitin-proteasome degradation, RNA polymerase II transcription, cell cycle regulation
MeSH terms: Animals, Catalysis, Cysteine Endopeptidases, Drug Stability, Gene Expression Regulation, Half-Life, HeLa Cells, Humans, Multienzyme Complexes, Phosphorylation, Ubiquitins, Cyclins, 3T3 Cells, Protein Serine-Threonine Kinases, Cyclin-Dependent Kinases, COS Cells, Proteasome Endopeptidase Complex, Mice, Cyclin C, Cyclin-Dependent Kinase 8

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Human cyclin C protein is stabilized by its associated kinase cdk8, independently of its catalytic activity

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