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Downregulation of COP9 signalosome subunits differentially affects the CSN complex and target protein stability by Andreas Peth; Christoph Berndt; Wolfgang Henke; Wolfgang Dubiel is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## 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. ## Results Permanent knockdowns of CSN1 and CSN3 led to a reduction of the subunits to approximately 40%, which is accompanied by a proportional decrease of the CSN holocomplex. In contrast, downregulation of CSN5 in HeLa cells reduced the CSN5 protein below 20% without significant effects on the remaining complex. The CRL component Rbx1 was characterized by accele

Who reads Downregulation of COP9 signalosome subunits differentially affects the CSN complex and target protein stability?

Author

Andreas Peth; Christoph Berndt; Wolfgang Henke; Wolfgang Dubiel

Publisher

BioMed Central; Springer (Biomed Central Ltd.); London: BioMed Central; Springer Science and Business Media LLC (ISSN 1471-2091)

Published

2007

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)