UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hong, Sunghoi | - |
dc.contributor.author | Lee, Soyeon | - |
dc.contributor.author | Cho, Ssang-Goo | - |
dc.contributor.author | Kang, Seongman | - |
dc.date.accessioned | 2021-09-09T07:19:49Z | - |
dc.date.available | 2021-09-09T07:19:49Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2008-06-27 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/123355 | - |
dc.description.abstract | UbcH6 is a member of an evolutionally conserved subfamily of E2 ubiquitin-conjugating enzymes. In this study, we report that UbcH6 interacts with and ubiquitinates ataxin-1, the spinocerebellar ataxia type 1 gene product. UbcH6 was identified as an ataxin-1-interacting protein using a yeast two-hybrid screen. UbcH6 co-immunoprecipitates and co-localizes with the ataxin-1 protein in the nucleus. Our binding assays showed that ataxin-1 interacts with UbcH6 through its AXH domain. Interestingly, UbcH6 could ubiquitinate ataxin-1 in the absence of an E3 ligase. The expression level of UbcH6 regulated the rate of ataxin-1 degradation. This study demonstrates that UbcH6 and ataxin-1 are E2-substrate cognate pairs in the ubiquitin-proteasome system. (C) 2008 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | RING-FINGER PROTEINS | - |
dc.subject | CONJUGATING ENZYME | - |
dc.subject | LIGASE ACTIVITY | - |
dc.subject | DEGRADATION | - |
dc.subject | PATHWAY | - |
dc.subject | DISEASE | - |
dc.subject | CLONING | - |
dc.subject | REPEAT | - |
dc.subject | TYPE-1 | - |
dc.subject | E6-AP | - |
dc.title | UbcH6 interacts with and ubiquitinates the SCA1 gene product ataxin-1 | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Hong, Sunghoi | - |
dc.contributor.affiliatedAuthor | Kang, Seongman | - |
dc.identifier.doi | 10.1016/j.bbrc.2008.04.066 | - |
dc.identifier.scopusid | 2-s2.0-43149123766 | - |
dc.identifier.wosid | 000256049700016 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.371, no.2, pp.256 - 260 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 371 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 256 | - |
dc.citation.endPage | 260 | - |
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.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | RING-FINGER PROTEINS | - |
dc.subject.keywordPlus | CONJUGATING ENZYME | - |
dc.subject.keywordPlus | LIGASE ACTIVITY | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | DISEASE | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | REPEAT | - |
dc.subject.keywordPlus | TYPE-1 | - |
dc.subject.keywordPlus | E6-AP | - |
dc.subject.keywordAuthor | ataxin-1 | - |
dc.subject.keywordAuthor | ubiquitination | - |
dc.subject.keywordAuthor | UbcH6 | - |
dc.subject.keywordAuthor | AXH domain | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
145 Anam-ro, Seongbuk-gu, Seoul, 02841, Korea+82-2-3290-2963
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.