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Mammalian COP9 signalosome
Author(s) -
Kato Junya,
YonedaKato Noriko
Publication year - 2009
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2009.01349.x
Subject(s) - cop9 signalosome , biology , ubiquitin ligase , ubiquitin , cullin , proteasome , deubiquitinating enzyme , microbiology and biotechnology , transcription factor , ubiquitin protein ligases , f box protein , transcriptional regulation , genetics , gene , biochemistry , enzyme , protease , peptide hydrolases
The COP9 signalosome (CSN) complex is highly conserved from yeast to human. Although the plant CSN was first identified as a negative regulator of photomorphogenesis, the mammalian CSN is linked to different biological responses such as checkpoint control, signal transduction, development and the cell cycle. Frequent over‐expression of the CSN subunit in a variety of human cancers suggests its involvement in cell transformation and tumorigenesis. The best‐known biochemical function associated with the CSN is the control of protein stability via the ubiquitin–proteasome system through regulation of cullin‐RING‐E3 ubiquitin ligase activity by deneddylation, by controlling the activity of COP1 E3 ligase, or by counteracting ubiquitin‐mediated degradation through a CSN‐associated deubiquitinating enzyme. In addition to affecting the stability of transcription factors, the CSN may regulate gene transcription by directly associating with chromatin. This review summarizes recent findings and discusses the physiological role and the cellular function of the mammalian CSN in terms of the regulation of cell proliferation.