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Updated: May 22, 2026

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae
Published on: April 18, 2016
Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation
Jessica R Blount1, Aaron A Burr, Amanda Denuc
1Department of Pharmacology and Department of Neurology, Wayne State University School of Medicine, Detroit, Michigan, United States of America.
Abstract:
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately delivered to the proteasome for degradation. It is not well understood how ubiquitination of ERAD substrates is regulated. Here, we present evidence that the deubiquitinating enzyme Ubiquitin-Specific Protease 25 (USP25) is involved in ERAD. Our data support a model where USP25 counteracts ubiquitination of ERAD substrates by the ubiquitin ligase HRD1, rescuing them from degradation by the proteasome.
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