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EMBO reports 3, 12, 1215–1221 (2002)
doi:10.1093/embo-reports/kvf235
Published online: December 2002
COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae
Vered Maytal-Kivity1, 3, Ron Piran1, 3, Elah Pick1, Kay Hofmann2 & Michael H. Glickman1
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1 Department of Biology and Institute for Catalysis Science and Technology (ICST), Technion–Israel Institute of Technology, 32000 Haifa, Israel
2 Bioinformatics Group, MEMOREC Stoffel GmbH, D-50829 Köln, Germany
3 V. Maytal-Kivity, R. Piran and E. Golan contributed equally to this work
To whom correspondence should be addressed
Michael H. Glickman Tel: +972 4 8294552; Fax: +972 4 8225153; glickman@tx.technion.ac.il
Received 11 July 2002; Accepted 30 September 2002.
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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.
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