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Eukaryotic Cell Jul (2008); 7(7):1191-9
Hos2p-Set3p deacetylase complex signals secretory stress through the Mpk1p cell integrity pathway-
Cohen TJ, Mallory MJ, Strich R, Yao TP
Department of Pharmacology and Cancer Biology, Duke University, Durham, NC 27710, USA-
Abstract: Perturbations in secretory function activate stress response pathways critical for yeast survival- Here we report the identification of the Hos2p-Set3p deacetylase complex -SET3C- as an essential component of the secretory stress response- Strains lacking core components of the Hos2p-Set3p complex exhibit hypersensitivity to secretory stress- Although not required for the unfolded protein response -UPR- and ribosomal gene repression, the Hos2p complex is required for proper activation of the Mpk1p-Slt2p cell integrity kinase cascade- Disruption of the Hos2p complex results in abrogated Mpk1p phosphorylation, whereas constitutive activation of the Mpk1p pathway rescues the hos2Delta mutant growth defect in response to secretory stress- Furthermore, Hos2p activity is required for the Mpk1p-mediated activation of stress-responsive transcription factor Rlm1p, but not for the stress-induced degradation of the C-type cyclin Ssn8p- Our results identify the Hos2p complex as a critical component of the secretory stress response and support the existence a coordinated stress response consisting of the UPR, ribosomal gene repression, and mitogen-activated protein kinase signaling in response to defects in secretory function-
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.