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• W2116777384 abstract "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." @default.
• W2116777384 created "2016-06-24" @default.
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• W2116777384 date "2002-12-01" @default.
• W2116777384 modified "2023-10-11" @default.
• W2116777384 title "COP9 signalosome components play a role in the mating pheromone response of <i>S. cerevisiae</i>" @default.
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• W2116777384 doi "https://doi.org/10.1093/embo-reports/kvf235" @default.
• W2116777384 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1319195" @default.
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