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FEBS Lett. 2015 Sep 14;589(19 Pt A):2507-13. doi: 10.1016/j.febslet.2015.06.007. Epub 2015 Jun 19.

Diversity of COP9 signalosome structures and functional consequences.

Author information

1
Institute of Experimental Internal Medicine, Medical Faculty, Otto von Guericke University, Leipziger Str. 44, 39120 Magdeburg, Germany.
2
Department of Molecular Structural Biology, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany.
3
Department of General, Visceral, Vascular and Thoracic Surgery, Division of Molecular Biology, Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany. Electronic address: wolfgang.dubiel@charite.de.

Abstract

The COP9 signalosome (CSN) is a regulator of the ubiquitin (Ub) proteasome system (UPS). It interacts with hundreds of cullin-RING ubiquitin E3 ligases (CRLs) and regulates their activity by removing the Ub-like protein Nedd8 from cullins. In mammalian cells 7 different cullins exist which form CRLs with adaptor proteins and with a large number of substrate recognition subunits such as F-box and BTB proteins. This large variety of CRL-complexes is deneddylated by the CSN. The capacity of the CSN to interact with numerous types of CRL complexes can be explained by its structural diversity, which allows different CSN variants to interact with different binding partners and substrates and enables different subunit expression profiles. Diversity of CSN complexes presumably occurs by: (1) flexibility of CSN holo complex structure; (2) formation of CSN mini complexes and free CSN subunits and (3) generation of CSN variants via integration of CSN subunit isoforms. In this review we will discuss the structural diversity of the CSN complex and possible functional consequences.

KEYWORDS:

3D structure; COP9 signalosome; CSN subunit isoform; CSN5; Deneddylation

PMID:
26096786
DOI:
10.1016/j.febslet.2015.06.007
[Indexed for MEDLINE]
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