Title: | COP9 signalosome components play a role in the mating pheromone response of S. cerevisiae |
Author(s): | Maytal-Kivity V; Piran R; Pick E; Hofmann K; Glickman MH; |
Address: | "Department of Biology and Institute for Catalysis Science and Technology, Technion-Israel Institute of Technology, 32000 Haifa, Israel" |
DOI: | 10.1093/embo-reports/kvf235 |
ISSN/ISBN: | 1469-221X (Print) 1469-3178 (Electronic) 1469-221X (Linking) |
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" |
Keywords: | COP9 Signalosome Complex Cell Cycle Proteins/metabolism *Cullin Proteins Multiprotein Complexes Peptide Hydrolases Pheromones/*metabolism Proteins/*metabolism Saccharomyces cerevisiae/*metabolism *Saccharomyces cerevisiae Proteins; |
Notes: | "MedlineMaytal-Kivity, Vered Piran, Ron Pick, Elah Hofmann, Kay Glickman, Michael H eng Research Support, Non-U.S. Gov't England 2002/11/26 EMBO Rep. 2002 Dec; 3(12):1215-21. doi: 10.1093/embo-reports/kvf235. Epub 2002 Nov 21" |