The devil is in the details: comparison between COP9 signalosome (CSN) and the LID of the 26S proteasome
Autor: | Miriam Kolog Gulko, Gerhard H. Braus, Anna M. Köhler, Cindy Meister |
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Rok vydání: | 2015 |
Předmět: |
0301 basic medicine
Proteasome Endopeptidase Complex Protein subunit Lysine Plasma protein binding NEDD8 Aspergillus nidulans 03 medical and health sciences Ubiquitin Genetics COP9 signalosome chemistry.chemical_classification Isopeptide bond biology COP9 Signalosome Complex General Medicine eye diseases Protein Subunits 030104 developmental biology chemistry Biochemistry Proteasome Multiprotein Complexes Mutation biology.protein sense organs Peptide Hydrolases Protein Binding |
Zdroj: | Current genetics. 62(1) |
ISSN: | 1432-0983 |
Popis: | The COP9 signalosome (CSN) and the proteasomal LID are conserved macromolecular complexes composed of at least eight subunits with molecular weights of approximately 350 kDa. CSN and LID are part of the ubiquitin–proteasome pathway and cleave isopeptide linkages of lysine side chains on target proteins. CSN cleaves the isopeptide bond of ubiquitin-like protein Nedd8 from cullins, whereas the LID cleaves ubiquitin from target proteins sentenced for degradation. CSN and LID are structurally and functionally similar but the order of the assembly pathway seems to be different. The assembly differs in at least the last subunit joining the pre-assembled subcomplex. This review addresses the similarities and differences in structure, function and assembly of CSN and LID. |
Databáze: | OpenAIRE |
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