SIRT1 deacetylates and stabilizes hypoxia-inducible factor-1 alpha (HIF-1 alpha) via direct interactions during hypoxia
DC Field | Value | Language |
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dc.contributor.author | Joo, Hyun-Yoo | - |
dc.contributor.author | Yun, Miyong | - |
dc.contributor.author | Jeong, Jaemin | - |
dc.contributor.author | Park, Eun-Ran | - |
dc.contributor.author | Shin, Hyun-Jin | - |
dc.contributor.author | Woo, Seon Rang | - |
dc.contributor.author | Jung, Jin Kyu | - |
dc.contributor.author | Kim, Yong-Min | - |
dc.contributor.author | Park, Joong-Jean | - |
dc.contributor.author | Kim, Joon | - |
dc.contributor.author | Lee, Kee-Ho | - |
dc.date.accessioned | 2021-09-04T14:17:34Z | - |
dc.date.available | 2021-09-04T14:17:34Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2015-07-10 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/93020 | - |
dc.description.abstract | Upon shift to a hypoxic environment, cellular HIF-1 alpha protein is stabilized, with a rapid decline in oxygen-sensitive hydroxylation. Several additional post-translational modifications of HIF-1 alpha are critical in controlling protein stability during hypoxia. In the present study, we showed that SIRT1 stabilizes HIF-1 alpha via direct binding and deacetylation during hypoxia. SIRT1 depletion or inactivation led to reduced hypoxic HIF-1 alpha accumulation, accompanied by an increase in HIF-1 alpha acetylation. Impaired HIF-1 alpha accumulation was recovered upon inhibition of 26S proteasome activity, indicating that SIRT1 is essential for HIF-1 alpha stabilization during hypoxia. Consistently, HIF-1 alpha accumulation was enhanced upon overexpression of wild-type SIRT1, but not its dominant-negative form. SIRT1-mediated accumulation of HIFI a protein led to increased expression of HIF-1 alpha target genes, including VEGF, GLUT1 and MMP2, and ultimate promotion of cancer cell invasion. These findings collectively imply that hypoxic HIF-1 alpha stabilization requires SIRT1 activation. Furthermore, SIRT1 protection of HIF-1 alpha from acetylation may be a prerequisite for stabilization and consequent enhancement of cell invasion. (C) 2015 Elsevier Inc. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.subject | PROTEIN-DEGRADATION | - |
dc.subject | FACTOR 1-ALPHA | - |
dc.subject | HIF-ALPHA | - |
dc.subject | HYDROXYLATION | - |
dc.subject | METABOLISM | - |
dc.subject | ACTIVATION | - |
dc.subject | MECHANISMS | - |
dc.subject | HIF1-ALPHA | - |
dc.subject | RESPONSES | - |
dc.title | SIRT1 deacetylates and stabilizes hypoxia-inducible factor-1 alpha (HIF-1 alpha) via direct interactions during hypoxia | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Park, Joong-Jean | - |
dc.contributor.affiliatedAuthor | Kim, Joon | - |
dc.identifier.doi | 10.1016/j.bbrc.2015.04.119 | - |
dc.identifier.scopusid | 2-s2.0-84930760040 | - |
dc.identifier.wosid | 000356560400003 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.462, no.4, pp.294 - 300 | - |
dc.relation.isPartOf | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 462 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 294 | - |
dc.citation.endPage | 300 | - |
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 | PROTEIN-DEGRADATION | - |
dc.subject.keywordPlus | FACTOR 1-ALPHA | - |
dc.subject.keywordPlus | HIF-ALPHA | - |
dc.subject.keywordPlus | HYDROXYLATION | - |
dc.subject.keywordPlus | METABOLISM | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordPlus | HIF1-ALPHA | - |
dc.subject.keywordPlus | RESPONSES | - |
dc.subject.keywordAuthor | SIRT1 | - |
dc.subject.keywordAuthor | HIF-1 alpha | - |
dc.subject.keywordAuthor | Stabilization | - |
dc.subject.keywordAuthor | Deacetylation | - |
dc.subject.keywordAuthor | Interaction | - |
dc.subject.keywordAuthor | Invasion | - |
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