COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae

Vered Maytal-Kivity, Ron Piran, Elah Pick, Kay Hofmann, Michael H. Glickman

Research output: Contribution to journalReview articlepeer-review

65 Scopus citations


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.

Original languageEnglish
Pages (from-to)1215-1221
Number of pages7
JournalEMBO Reports
Issue number12
StatePublished - 1 Dec 2002
Externally publishedYes


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