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2012-05

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cc-by (c) Blount, J.R. et al., 2012
Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/43320

Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation

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http://dx.doi.org/10.1371/journal.pone.0036542

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.

Subject

Proteïnes, Enzims, Reticle endoplasmàtic

Subject (English)

Proteins, Enzymes, Endoplasmic reticulum

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Articles publicats en revistes (Genètica, Microbiologia i Estadística)

Citation

BLOUNT, J. R., et al. Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation. PLoS One. 2012. Vol. 7, num. 5, pags. e36542. ISSN 1932-6203. [consulted: 7 of August of 2026]. Available at: https://hdl.handle.net/2445/43320

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