Journal of Cell Science 115, e302-e302 (2002)
© 2002 The Company of Biologists Limited
The COP9 signalosome (p. 467)
The COP9 signalosome (CSN) is a protein complex whose eight subunits
display significant sequence similarity to those of the 26S proteasome LID
a component of the 26S proteasome complex that degrades
ubiquitin-conjugated proteins. What is the function of this LID-like
structure? Wolfgang Dubiel and co-workers examine studies suggesting that it
functions as a platform that connects signalling with proteolysis. First
identified as being important for proper plant photomorphogenesis, the CSN
appears to control many aspects of plant development. It is also implicated in
regulation of the yeast cell cycle and fruitfly development. Recent work
suggests that the CSN cooperates with the E3 ubiquitin ligase SCF to control
stability of key cell cycle and developmental regulators. Furthermore, one of
its subunits, CSN5, has been shown to interact with a variety of cellular
regulators, including the CDK inhibitor p27Kip1 and the
transcription factor JUN. Indeed, such molecules might be targets of a
CSN-associated kinase that targets them for degradation by the ubiquitin
system.

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Related articles in JCS:
- The COP9 signalosome: at the interface between signal transduction and ubiquitin-dependent proteolysis
- Dawadschargal Bech-Otschir, Michael Seeger, and Wolfgang Dubiel
JCS 2002 115: 467-473.
[Abstract]
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