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Authordc.contributor.authorQuiroga, Clara 
Authordc.contributor.authorGatica, Damián 
Authordc.contributor.authorParedes, Felipe 
Authordc.contributor.authorBravo, Roberto 
Authordc.contributor.authorTroncoso, Rodrigo 
Authordc.contributor.authorPedrozo Cibils, Zully 
Authordc.contributor.authorRodríguez, Andrea E. 
Authordc.contributor.authorToro, Barbra 
Authordc.contributor.authorChiong Lay, Mario 
Authordc.contributor.authorVicencio Bustamante, José Manuel 
Authordc.contributor.authorHetz Flores, Claudio 
Authordc.contributor.authorLavandero González, Sergio 
Admission datedc.date.accessioned2019-03-15T16:06:03Z
Available datedc.date.available2019-03-15T16:06:03Z
Publication datedc.date.issued2013
Cita de ítemdc.identifier.citationBiochimica et Biophysica Acta - Molecular Cell Research, Volumen 1833, Issue 12, 2018, Pages 3295-3305
Identifierdc.identifier.issn18792596
Identifierdc.identifier.issn01674889
Identifierdc.identifier.other10.1016/j.bbamcr.2013.09.006
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/166103
Abstractdc.description.abstractHerp is an endoplasmic reticulum (ER) stress inducible protein that participates in the ER-associated protein degradation (ERAD) pathway. However, the contribution of Herp to other protein degradation pathways like autophagy and its connection to other types of stress responses remain unknown. Here we report that Herp regulates autophagy to clear poly-ubiquitin (poly-Ub) protein aggregates. Proteasome inhibition and glucose starvation (GS) led to a high level of poly-Ub protein aggregation that was drastically reduced by stably knocking down Herp (shHerp cells). The enhanced removal of poly-Ub inclusions protected cells from death caused by glucose starvation. Under basal conditions and increasingly after stress, higher LC3-II levels and GFP-LC3 puncta were observed in shHerp cells compared to control cells. Herp knockout cells displayed basal up-regulation of two essential autophagy regulators-Atg5 and Beclin-1, leading to increased autophagic flux. Beclin-1 up-regulation was due to a
Lenguagedc.language.isoen
Publisherdc.publisherElsevier
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Sourcedc.sourceBiochimica et Biophysica Acta - Molecular Cell Research
Keywordsdc.subjectAutophagy
Keywordsdc.subjectBeclin-1
Keywordsdc.subjectEndoplasmic reticulum stress
Keywordsdc.subjectPoly-ubiquitinated protein
Keywordsdc.subjectProtein aggregation
Keywordsdc.subjectUPR
Títulodc.titleHerp depletion protects from protein aggregation by up-regulating autophagy
Document typedc.typeArtículo de revista
dcterms.accessRightsdcterms.accessRightsAcceso Abierto
Catalogueruchile.catalogadorSCOPUS
Indexationuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile