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.
Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation
Jessica R. Blount,Aaron A. Burr,A. Denuc,G. Marfany,Sokol V. Todi
Published 2012 in PLoS ONE
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PUBLICATION RECORD
- Publication year
2012
- Venue
PLoS ONE
- Publication date
2012-05-09
- Fields of study
Biology, Medicine
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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