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A more recent version of this article appeared on November 1, 2007
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Submitted on May 24, 2007
Revised on July 13, 2007
Accepted on August 8, 2007
Department of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, OR 97239
Monitoring Editor: Jonathan Weissman
ER-associated, ubiquitin-proteasome system (UPS)-mediated degradation of the wild-type gap junction protein connexin32 (WT Cx32) is inhibited by mild forms of cytosolic stress at a step before its dislocation into the cytosol. We show that the same conditions (a 30 min, 42°C heat shock or oxidative stress induced by arsenite) also reduce the ER-associated turnover of disease-causing mutants of Cx32 and CFTR, as well as that of WT CFTR and unassembled Ig light chain. Stress-stabilized WT Cx32 and CFTR, but not the mutant/unassembled proteins examined, could traverse the secretory pathway. Heat shock also slowed the otherwise rapid UPS-mediated turnover of the cytosolic proteins myoD and GFPu, but not the degradation of an ubiquitination-independent construct (GFP-ODC) closely related to the latter. Analysis of mutant Cx32 from cells exposed to proteasome inhibitors and/or cytosolic stress indicated that stress reduces degradation at the level of substrate polyubiquitination. These findings reveal a new link between the cytosolic stress-induced heat shock response, ER-associated degradation, and polyubiquitination. Stress-denatured proteins may titer a limiting component of the ubiquitination machinery away from pre-existing UPS substrates, thereby sparing the latter from degradation.
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