Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/43320
Title: Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation
Author: Blount, J. R.
Burr, A. A.
Denuc Isern, Amanda
Marfany i Nadal, Gemma
Todi, S. V.
Keywords: Proteïnes
Enzims
Reticle endoplasmàtic
Proteins
Enzymes
Endoplasmic reticulum
Issue Date: May-2012
Publisher: Public Library of Science (PLoS)
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.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0036542
It is part of: PLoS One, 2012, vol. 7, num. 5, p. e36542
Related resource: http://dx.doi.org/10.1371/journal.pone.0036542
URI: http://hdl.handle.net/2445/43320
ISSN: 1932-6203
Appears in Collections:Articles publicats en revistes (Genètica, Microbiologia i Estadística)

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