Reference : KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
KCTD5, a putative substrate adaptor for cullin3 ubiquitin ligases
Bayón, Yolanda [Université de Liège - ULiège > Département des sciences cliniques > GIGA-R:Immunopath. - Maladies infect. et médec. inter. gén. >]
Trinidad, Antonio G. [> > > >]
de la Puerta, María L [> > > >]
del Carmen Rodríguez, María [> > > >]
Bogetz, Jori [> > > >]
Rojas, Ana [> > > >]
De Pereda, José [> > > >]
Rahmouni, Souad mailto [> > > >]
Williams, Scott [> > > >]
Matsuzawa, Shu-ichi [> > > >]
Reed, John C [> > > >]
Sánchez Crespo, Mariano [> > > >]
Mustelin, Tomas [> > > >]
Alonso, Andres [> > > >]
FEBS Journal
Blackwell Publishing
3900 - 3910
Yes (verified by ORBi)
United Kingdom
[en] BTB ; Cullin ; E3 ligases
[fr] KCTD ; Ubiquitin
[en] Potassium channel tetramerization domain (KCTD) proteins contain a bric-a-brac, tramtrak and broad complex (BTB) domain that is most similar to the tetramerization domain (T1) of voltage-gated potassium channels. Some BTB-domain-containing proteins have been shown recently to participate as substrate-specific adaptors in multimeric cullin E3 ligase reactions by recruiting proteins for ubiquitination and subsequent degradation by the proteasome. Twenty-two KCTD proteins have been found in the human genome, but their functions are largely unknown. In this study, we have characterized KCTD5, a new KCTD protein found in the cytosol of cultured cell lines. The expression of KCTD5 was upregulated post-transcriptionally in peripheral blood lymphocytes stimulated through the T-cell receptor. KCTD5 interacted specifically with cullin3, bound ubiquitinated proteins, and formed oligomers through its BTB domain. Analysis of the interaction with cullin3 showed that, in addition to the BTB domain, some amino acids in the N-terminus of KCTD5 are required for binding to cullin3. These findings suggest that KCTD5 is a substrate-specific adaptor for cullin3-based E3 ligases.
Instituto de Biología y Genética Molecular, CSIC-Universidad de Valladolid, Spain.
This work was supported by a grant from Programa Nacional de Biología Fundamental (Grant BFU2006-01203/BMC), Red Cardiovascular from Instituto de Salud Carlos III. Y. Bayón is under contract within the Ramón y Cajal Program of the Ministerio de Educación y Ciencia of Spain, co-funded by the European Social Fund through FEDER-FSE.
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