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COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae
Author(s) -
MaytalKivity Vered,
Piran Ron,
Pick Elah,
Hofmann Kay,
Glickman Michael H.
Publication year - 2002
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kvf235
Subject(s) - cop9 signalosome , biology , saccharomyces cerevisiae , proteasome , pheromone , phenotype , interactor , protein subunit , genetics , microbiology and biotechnology , cullin , regulator , yeast , ubiquitin , gene , biochemistry , ubiquitin ligase , protease , peptide hydrolases , enzyme
A family of genetically and structurally homologous complexes, the proteasome lid, Cop9 signalosome (CSN) and eukaryotic translation initiation factor 3, mediate different regulatory pathways. The CSN functions in numerous eukaryotes as a regulator of development and signaling, yet until now no evidence for a complex has been found in Saccharomyces cerevisiae . We identified a group of proteins, including a homolog of Csn5/Jab1 and four uncharacterized PCI components, that interact in a manner suggesting they form a complex analogous to the CSN in S. cerevisiae . These newly identified subunits play a role in adaptation to pheromone signaling. Deletants for individual subunits enhance pheromone response and increase mating efficiency. Overexpression of individual subunits or a human homolog mitigates sst2 ‐induced pheromone sensitivity. Csi1, a novel CSN interactor, exhibits opposite phenotypes. Deletants also accumulate Cdc53/cullin in a Rub1‐modified form; however, this role of the CSN appears to be distinct from that in the mating pathway.