Modulation of SQSTM1/p62 activity by N-terminal arginylation of the endoplasmic reticulum chaperone HSPA5/GRP78/BiP
DC Field | Value | Language |
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dc.contributor.author | Cha-Molstad, Hyunjoo | - |
dc.contributor.author | Yu, Ji Eun | - |
dc.contributor.author | Lee, Su Hyun | - |
dc.contributor.author | Kim, Jung Gi | - |
dc.contributor.author | Sung, Ki Sa | - |
dc.contributor.author | Hwang, Joonsung | - |
dc.contributor.author | Yoo, Young Dong | - |
dc.contributor.author | Lee, Yoon Jee | - |
dc.contributor.author | Kim, Sung Tae | - |
dc.contributor.author | Lee, Dae Hee | - |
dc.contributor.author | Ciechanover, Aaron | - |
dc.contributor.author | Kim, Bo Yeon | - |
dc.contributor.author | Kwon, Yong Tae | - |
dc.date.accessioned | 2021-09-04T04:58:36Z | - |
dc.date.available | 2021-09-04T04:58:36Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2016 | - |
dc.identifier.issn | 1554-8627 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/90132 | - |
dc.description.abstract | The 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.language | English | - |
dc.language.iso | en | - |
dc.publisher | TAYLOR & FRANCIS INC | - |
dc.title | Modulation of SQSTM1/p62 activity by N-terminal arginylation of the endoplasmic reticulum chaperone HSPA5/GRP78/BiP | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Lee, Dae Hee | - |
dc.identifier.doi | 10.1080/15548627.2015.1126047 | - |
dc.identifier.scopusid | 2-s2.0-84964483788 | - |
dc.identifier.wosid | 000373982600017 | - |
dc.identifier.bibliographicCitation | AUTOPHAGY, v.12, no.2, pp.426 - 428 | - |
dc.relation.isPartOf | AUTOPHAGY | - |
dc.citation.title | AUTOPHAGY | - |
dc.citation.volume | 12 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 426 | - |
dc.citation.endPage | 428 | - |
dc.type.rims | ART | - |
dc.type.docType | Editorial Material | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordAuthor | ATE1 R-transferase | - |
dc.subject.keywordAuthor | N-end rule pathway | - |
dc.subject.keywordAuthor | protein arginylation | - |
dc.subject.keywordAuthor | protein quality control | - |
dc.subject.keywordAuthor | proteolysis | - |
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