Selenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Jea Hwang | - |
dc.contributor.author | Park, Ki Jun | - |
dc.contributor.author | Jang, Jun Ki | - |
dc.contributor.author | Jeon, Yeong Ha | - |
dc.contributor.author | Ko, Kwan Young | - |
dc.contributor.author | Kwon, Joon Hyun | - |
dc.contributor.author | Lee, Seung-Rock | - |
dc.contributor.author | Kim, Ick Young | - |
dc.date.accessioned | 2021-09-04T09:18:05Z | - |
dc.date.available | 2021-09-04T09:18:05Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2015-12-11 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/91580 | - |
dc.description.abstract | Cytosolic valosin-containing protein (p97(VCP)) is translocated to the ER membrane by binding to selenoprotein S (SelS), which is an ER membrane protein, during endoplasmic reticulum-associated degradation (ERAD). Selenoprotein K (SelK) is another known p97(VCP)-binding selenoprotein, and the expression of both SelS and SelK is increased under ER stress. To understand the regulatory mechanisms of SelS, SelK, and p97(VCP) during ERAD, the interaction of the selenoproteins with p97(VCP) was investigated using N2a cells and HEK293 cells. Both SelS and SelK co-precipitated with p97(VCP). However, the association between SelS and SelK did not occur in the absence of p97(VCP). SelS had the ability to recruit p97(VCP) to the ER membrane but SelK did not. The interaction between SelK and p97(VCP) did not occur in SelS knockdown cells, whereas SelS interacted with p97(VCP) in the presence or absence of SelK. These results suggest that p97(VCP) is first translocated to the ER membrane via its interaction with SelS, and then SelK associates with the complex on the ER membrane. Therefore, the interaction between SelK and p97(VCP) is SelS-dependent, and the resulting ERAD complex (SelS-p97(VCP)-SelK) plays an important role in ERAD and ER stress. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | AAA-ATPASE | - |
dc.subject | MULTIPROTEIN COMPLEXES | - |
dc.subject | QUALITY-CONTROL | - |
dc.subject | PHYSIOLOGICAL ROLES | - |
dc.subject | INDUCED APOPTOSIS | - |
dc.subject | UBIQUITIN LIGASE | - |
dc.subject | STRESS | - |
dc.subject | ER | - |
dc.subject | MEMBRANE | - |
dc.subject | CELLS | - |
dc.title | Selenoprotein S-dependent Selenoprotein K Binding to p97(VCP) Protein Is Essential for Endoplasmic Reticulum-associated Degradation | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Ick Young | - |
dc.identifier.doi | 10.1074/jbc.M115.680215 | - |
dc.identifier.scopusid | 2-s2.0-84949662465 | - |
dc.identifier.wosid | 000366614700026 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.290, no.50, pp.29941 - 29952 | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 290 | - |
dc.citation.number | 50 | - |
dc.citation.startPage | 29941 | - |
dc.citation.endPage | 29952 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | AAA-ATPASE | - |
dc.subject.keywordPlus | MULTIPROTEIN COMPLEXES | - |
dc.subject.keywordPlus | QUALITY-CONTROL | - |
dc.subject.keywordPlus | PHYSIOLOGICAL ROLES | - |
dc.subject.keywordPlus | INDUCED APOPTOSIS | - |
dc.subject.keywordPlus | UBIQUITIN LIGASE | - |
dc.subject.keywordPlus | STRESS | - |
dc.subject.keywordPlus | ER | - |
dc.subject.keywordPlus | MEMBRANE | - |
dc.subject.keywordPlus | CELLS | - |
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.