Maytal-Kivity V, et al. (2002) COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae. EMBO Rep 3(12):1215-21
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.
| Status: Published | Type: Journal Article | PubMed ID: 12446563 |
Topics addressed in this paper
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| CDC53 | CSI1 | CSN9 | PCI8 | RRI1 | RRI2 | RUB1 | SST2 | YJR084W | |
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