Please use this identifier to cite or link to this item: http://hdl.handle.net/10553/35318
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dc.contributor.authorZhang, Lien_US
dc.contributor.authorRajbhandari, Prashanten_US
dc.contributor.authorPriest, Christinaen_US
dc.contributor.authorSandhu, Jaspreeten_US
dc.contributor.authorWu, Xiaohuien_US
dc.contributor.authorTemel, Ryanen_US
dc.contributor.authorCastrillo Viguera, Antonioen_US
dc.contributor.authorDe Aguiar Vallim, Thomas Q.en_US
dc.contributor.authorSallam, Tameren_US
dc.contributor.authorTontonoz, Peteren_US
dc.date.accessioned2018-04-02T10:58:55Z-
dc.date.available2018-04-02T10:58:55Z-
dc.date.issued2017en_US
dc.identifier.issn2050-084Xen_US
dc.identifier.urihttp://hdl.handle.net/10553/35318-
dc.description.abstractCholesterol homeostasis is maintained through concerted action of the\r\nSREBPs and LXRs. Here, we report that RNF145, a previously\r\nuncharacterized ER membrane ubiquitin ligase, participates in crosstalk\r\nbetween these critical signaling pathways. RNF145 expression is induced\r\nin response to LXR activation and high-cholesterol diet feeding.\r\nTransduction of RNF145 into mouse liver inhibits the expression of genes\r\ninvolved in cholesterol biosynthesis and reduces plasma cholesterol\r\nlevels. Conversely, acute suppression of RNF145 via shRNA-mediated\r\nknockdown, or chronic inactivation of RNF145 by genetic deletion,\r\npotentiates the expression of cholesterol biosynthetic genes and\r\nincreases cholesterol levels both in liver and plasma. Mechanistic\r\nstudies show that RNF145 triggers ubiquitination of SCAP on lysine\r\nresidues within a cytoplasmic loop essential for COPII binding,\r\npotentially inhibiting its transport to Golgi and subsequent processing\r\nof SREBP-2. These findings define an additional mechanism linking\r\nhepatic sterol levels to the reciprocal actions of the SREBP-2 and LXR\r\npathways.en_US
dc.languageengen_US
dc.relation.ispartofeLifeen_US
dc.sourceeLife [ISSN 2050-084X], v. 6, e28766, (Octubre 2017)en_US
dc.subject320502 Endocrinologíaen_US
dc.subject2407 Biología celularen_US
dc.subject3206 Ciencias de la nutriciónen_US
dc.subject.otherLiver-X-Receptoren_US
dc.subject.otherCleavage-Activating proteinen_US
dc.subject.otherHMG coa reductaseen_US
dc.subject.otherLXR-Alphaen_US
dc.subject.otherDeficient miceen_US
dc.subject.otherLipid-Metabolismen_US
dc.subject.otherLDL receptoren_US
dc.subject.otherSrebpen_US
dc.subject.otherGeneen_US
dc.subject.otherPathwayen_US
dc.titleInhibition of cholesterol biosynthesis through RNF145-dependent ubiquitination of SCAPen_US
dc.typeinfo:eu-repo/semantics/Articleen_US
dc.typeArticleen_US
dc.identifier.doi10.7554/eLife.28766.001en_US
dc.identifier.scopus2-s2.0-85032987153-
dc.identifier.isi000413723800001-
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dc.identifier.eissn2050-084X-
dc.relation.volume6en_US
dc.investigacionCiencias de la Saluden_US
dc.source.typear-
dc.type2Artículoen_US
dc.contributor.daisngid173268-
dc.contributor.daisngid2323857-
dc.contributor.daisngid3505355-
dc.contributor.daisngid11306-
dc.contributor.daisngid30309796-
dc.contributor.daisngid30316522-
dc.contributor.daisngid225640-
dc.contributor.daisngid1325985-
dc.contributor.daisngid1460009-
dc.contributor.daisngid103250-
dc.description.numberofpages20en_US
dc.utils.revisionen_US
dc.contributor.wosstandardWOS:Zhang, L-
dc.contributor.wosstandardWOS:Rajbhandari, P-
dc.contributor.wosstandardWOS:Priest, C-
dc.contributor.wosstandardWOS:Sandhu, J-
dc.contributor.wosstandardWOS:Wu, XH-
dc.contributor.wosstandardWOS:Temel, R-
dc.contributor.wosstandardWOS:Castrillo, A-
dc.contributor.wosstandardWOS:Vallim, TQD-
dc.contributor.wosstandardWOS:Sallam, T-
dc.contributor.wosstandardWOS:Tontonoz, P-
dc.date.coverdateOctubre 2017en_US
dc.identifier.ulpgcen_US
dc.contributor.buulpgcBU-MEDen_US
dc.description.sjr7,121
dc.description.jcr7,616
dc.description.sjrqQ1
dc.description.jcrqQ1
dc.description.scieSCIE
item.grantfulltextopen-
item.fulltextCon texto completo-
crisitem.author.orcid0000-0002-2057-2159-
crisitem.author.fullNameCastrillo Viguera, Antonio Jesús-
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