Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kwon, Do Hoon | - |
dc.contributor.author | Park, Ok Hyun | - |
dc.contributor.author | Kim, Leehyeon | - |
dc.contributor.author | Jung, Yang Ouk | - |
dc.contributor.author | Park, Yeonkyoung | - |
dc.contributor.author | Jeong, Hyeongseop | - |
dc.contributor.author | Hyun, Jaekyung | - |
dc.contributor.author | Kim, Yoon Ki | - |
dc.contributor.author | Song, Hyun Kyu | - |
dc.date.accessioned | 2021-09-02T07:39:26Z | - |
dc.date.available | 2021-09-02T07:39:26Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2018-08-17 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/73751 | - |
dc.description.abstract | p62/SQSTM1 is the key autophagy adapter protein and the hub of multi-cellular signaling. It was recently reported that autophagy and N-end rule pathways are linked via p62. However, the exact recognition mode of degrading substrates and regulation of p62 in the autophagic pathway remain unknown. Here, we present the complex structures between the ZZ-domain of p62 and various type-1 and type-2 N-degrons. The binding mode employed in the interaction of the ZZ-domain with N-degrons differs from that employed by classic N-recognins. It was also determined that oligomerization via the PB1 domain can control functional affinity to the R-BiP substrate. Unexpectedly, we found that self-oligomerization and disassembly of p62 are pH-dependent. These findings broaden our understanding of the functional repertoire of the N-end rule pathway and provide an insight into the regulation of p62 during the autophagic pathway. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.subject | STRUCTURAL BASIS | - |
dc.subject | UBIQUITIN-BINDING | - |
dc.subject | P62 | - |
dc.subject | PROTEIN | - |
dc.subject | RECOGNITION | - |
dc.subject | PATHWAY | - |
dc.subject | DOMAIN | - |
dc.subject | SYSTEM | - |
dc.subject | SPECIFICITY | - |
dc.subject | PHENIX | - |
dc.title | Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Yoon Ki | - |
dc.contributor.affiliatedAuthor | Song, Hyun Kyu | - |
dc.identifier.doi | 10.1038/s41467-018-05825-x | - |
dc.identifier.scopusid | 2-s2.0-85051621773 | - |
dc.identifier.wosid | 000441865400005 | - |
dc.identifier.bibliographicCitation | NATURE COMMUNICATIONS, v.9 | - |
dc.relation.isPartOf | NATURE COMMUNICATIONS | - |
dc.citation.title | NATURE COMMUNICATIONS | - |
dc.citation.volume | 9 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Science & Technology - Other Topics | - |
dc.relation.journalWebOfScienceCategory | Multidisciplinary Sciences | - |
dc.subject.keywordPlus | STRUCTURAL BASIS | - |
dc.subject.keywordPlus | UBIQUITIN-BINDING | - |
dc.subject.keywordPlus | P62 | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | RECOGNITION | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | PHENIX | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(02841) 서울특별시 성북구 안암로 14502-3290-1114
COPYRIGHT © 2021 Korea University. All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.