Modulation of SQSTM1/p62 activity by N-terminal arginylation of the endoplasmic reticulum chaperone HSPA5/GRP78/BiP

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dc.contributor.authorHyunjoo Cha-
dc.contributor.authorJi-Eun Yu-
dc.contributor.authorSu Hyun Lee-
dc.contributor.authorJung Gi Kim-
dc.contributor.authorK S Sung-
dc.contributor.authorJoonsung Hwang-
dc.contributor.authorY D Yoo-
dc.contributor.authorY J Lee-
dc.contributor.authorS T Kim-
dc.contributor.authorD H Lee-
dc.contributor.authorA Ciechanover-
dc.contributor.authorBo Yeon Kim-
dc.contributor.authorY T Kwon-
dc.date.accessioned2017-04-19T10:19:02Z-
dc.date.available2017-04-19T10:19:02Z-
dc.date.issued2016-
dc.identifier.issn15548627-
dc.identifier.uri10.1080/15548627.2015.1126047ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/13196-
dc.description.abstractThe N-end rule pathway is a proteolytic system, in which single N-terminal residues act as a determinant of a class of degrons, called N-degrons. In the ubiquitin (Ub)-proteasome system, specific recognition components, called N-recognins, recognize N-degrons and accelerate polyubiquitination and proteasomal degradation of the substrates. In this study, we show that the pathway regulates the activity of the macroautophagic receptor SQSTM1/p62 (sequestosome 1) through N-terminal arginylation (Nt-arginylation) of endoplasmic reticulum (ER)-residing molecular chaperones, including HSPA5/GRP78/BiP, CALR (calreticulin), and PDI (protein disulfide isomerase). The arginylation is co-induced with macroautophagy (hereafter autophagy) as part of innate immunity to cytosolic DNA and when misfolded proteins accumulate under proteasomal inhibition. Following cytosolic relocalization and arginylation, Nt-arginylated HSPA5 (R-HSPA5) is targeted to autophagosomes and degraded by lysosomal hydrolases through the interaction of its N-terminal Arg (Nt-Arg) with ZZ domain of SQSTM1. Upon binding to Nt-Arg, SQSTM1 undergoes a conformational change, which promotes SQSTM1 self-polymerization and interaction with LC3, leading to SQSTM1 targeting to autophagosomes. Cargoes of R-HSPA5 include cytosolic misfolded proteins destined to be degraded through autophagy. Here, we discuss the mechanisms by which the N-end rule pathway regulates SQSTM1-dependent selective autophagy.-
dc.publisherT&F (Taylor & Francis)-
dc.titleModulation of SQSTM1/p62 activity by N-terminal arginylation of the endoplasmic reticulum chaperone HSPA5/GRP78/BiP-
dc.title.alternativeModulation of SQSTM1/p62 activity by N-terminal arginylation of the endoplasmic reticulum chaperone HSPA5/GRP78/BiP-
dc.typeArticle-
dc.citation.titleAutophagy-
dc.citation.number2-
dc.citation.endPage428-
dc.citation.startPage426-
dc.citation.volume12-
dc.contributor.affiliatedAuthorHyunjoo Cha-
dc.contributor.affiliatedAuthorJoonsung Hwang-
dc.contributor.affiliatedAuthorBo Yeon Kim-
dc.contributor.alternativeName차현주-
dc.contributor.alternativeName유지은-
dc.contributor.alternativeName이수현-
dc.contributor.alternativeName김정기-
dc.contributor.alternativeName성기사-
dc.contributor.alternativeName황준성-
dc.contributor.alternativeName유영동-
dc.contributor.alternativeName이윤지-
dc.contributor.alternativeName김성태-
dc.contributor.alternativeName이대희-
dc.contributor.alternativeNameCiechanover-
dc.contributor.alternativeName김보연-
dc.contributor.alternativeName권용태-
dc.identifier.bibliographicCitationAutophagy, vol. 12, no. 2, pp. 426-428-
dc.identifier.doi10.1080/15548627.2015.1126047-
dc.subject.keywordATE1 R-transferase-
dc.subject.keywordN-end rule pathway-
dc.subject.keywordprotein arginylation-
dc.subject.keywordprotein quality control-
dc.subject.keywordproteolysis-
dc.subject.localATE1 R-transferase-
dc.subject.localN-end rule pathway-
dc.subject.localprotein arginylation-
dc.subject.localprotein quality control-
dc.subject.localproteolysis-
dc.subject.localProteolysis-
dc.description.journalClassY-
Appears in Collections:
Ochang Branch Institute > Anticancer Agent Research Center > 1. Journal Articles
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