Abstract
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.
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We thank Josua Schinke and Bastian Joehnk for critically reading the manuscript and Gabriele Heinrich for excellent technical support. We apologize to those authors whose contributions could not be cited due to space limitation. Work in our lab is supported by the Deutsche Forschungsgemeinschaft (DFG) within the SFB860.
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Communicated by M. Kupiec.
C. Meister, M. Kolog Gulko, and A.M. Köhler equally contributed to this work.
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Meister, C., Kolog Gulko, M., Köhler, A.M. et al. The devil is in the details: comparison between COP9 signalosome (CSN) and the LID of the 26S proteasome. Curr Genet 62, 129–136 (2016). https://doi.org/10.1007/s00294-015-0525-7
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DOI: https://doi.org/10.1007/s00294-015-0525-7