Downregulation of COP9 signalosome subunits differentially affects the CSN complex and target protein stability |
| |
| Authors: | Andreas Peth Christoph Berndt Wolfgang Henke Wolfgang Dubiel |
| |
| Affiliation: | 1.Department of Surgery, Division of Molecular Biology,Charité – Universit?tsmedizin Berlin,Berlin,Germany;2.Department of Otorhinolaryngology, Molecular Biology Research Laboratory,Charité – Universit?tsmedizin Berlin,Berlin,Germany |
| |
| Abstract: | Background The COP9 signalosome (CSN) is a conserved protein complex in eukaryotic cells consisting of eight subunits (CSN1 to CSN8). Recent data demonstrate that the CSN is a regulator of the ubiquitin (Ub) proteasome system (UPS). It controls substrate ubiquitination by cullin-RING Ub ligases (CRLs), a process that determines substrate specificity of the UPS. The intrinsic deneddylating activity localized to CSN5 as well as the associated kinases and deubiquitinating activity are involved in the regulatory function of CSN. The exact mechanisms are unclear. In this study we knocked down CSN1 (siCSN1), CSN3 (siCSN3) and CSN5 (siCSN5) by specific siRNA oligos permanently expressed in HeLa cells. The analysis and comparison of siRNA cells revealed differential impact of individual subunits on CSN structure and function. |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
