TY - JOUR
T1 - COP9 signalosome revisited
T2 - A novel mediator of protein degradation
AU - Schwechheimer, Claus
AU - Deng, Xing Wang
N1 - Funding Information:
We thank G. Serino for comments on the manuscript and N. Wei for help with Fig. 1 . Our research is supported by an NSF grant (MCD-00777217) and a BARD (IS-3123-99) grant to X-W. Deng. C. Schwechheimer was a fellow of the Deutsche Forschungsgemeinschaft (Schw751-1/1).
PY - 2001/10/1
Y1 - 2001/10/1
N2 - The COP9 signalosome is an evolutionarily conserved multiprotein complex that was first identified as an essential complex that represses light-regulated development in Arabidopsis. The COP9 signalosome has similarity to the lid of the 19S regulatory particle of the 26S proteasome and has recently been shown to interact with SCF-type E3 ubiquitin ligases. Although its precise role in the process of protein degradation remains to be established, the COP9 signalosome is a positive regulator of E3 ubiquitin ligases that functions at least in part by mediating the deconjugation of the NEDD8/RUB-modification from the cullin subunit of SCF-type E3 complexes. Here, we discuss these recent findings, which add an additional component to the biology of substrate-specific protein degradation.
AB - The COP9 signalosome is an evolutionarily conserved multiprotein complex that was first identified as an essential complex that represses light-regulated development in Arabidopsis. The COP9 signalosome has similarity to the lid of the 19S regulatory particle of the 26S proteasome and has recently been shown to interact with SCF-type E3 ubiquitin ligases. Although its precise role in the process of protein degradation remains to be established, the COP9 signalosome is a positive regulator of E3 ubiquitin ligases that functions at least in part by mediating the deconjugation of the NEDD8/RUB-modification from the cullin subunit of SCF-type E3 complexes. Here, we discuss these recent findings, which add an additional component to the biology of substrate-specific protein degradation.
UR - http://www.scopus.com/inward/record.url?scp=0035478483&partnerID=8YFLogxK
U2 - 10.1016/S0962-8924(01)02091-8
DO - 10.1016/S0962-8924(01)02091-8
M3 - Review article
C2 - 11567875
AN - SCOPUS:0035478483
SN - 0962-8924
VL - 11
SP - 420
EP - 426
JO - Trends in Cell Biology
JF - Trends in Cell Biology
IS - 10
ER -