A complex containing βTrCP recruits Ccd34 to catalyse ubiquitination of IκBα

FEBS Letters

Hay, Ronald T¹  Nicholson, John¹  Vuillard, Laurent¹ 

[1] School of Biomedical Science, BMS Building, University of St. Andrews, St. Andrews, Fife KY16 9ST, UK

关键词: IκBα ubiquitination;    NF-κB activation;    βTrCP;    SCF ubiquitin ligase;   

DOI  :  10.1016/S0014-5793(99)00895-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Activation of transcription factor NF-κB is accomplished by degradation of its inhibitor IκBα. Signal induced phosphorylation of IκBα on serine 32 and 36 targets the protein for ubiquitination on lysine 21 and 22. Here we use a phosphorylated peptide substrate representing residues 20–43 of IκBα to investigate requirements for ubiquitination of IκBα. Phosphorylation dependent polyubiquitination is carried out by a multiprotein complex containing βTrCP, Skp1 and Cdc53 (Cul1). In the presence of ubiquitin activating enzyme and the protein complex containing βTrCP, polyubiquitination of IκBα peptide was dependent on the presence of Cdc34, while Ubc5 only stimulated mono- and di-ubiquitination.

【 授权许可】

Unknown