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Differential responses of two degradation domains of HIF-1alpha to hypoxia and iron deficiency
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Kyoung-Hwa | - |
dc.contributor.author | Choi, Eunjoo | - |
dc.contributor.author | Chun, Yang-Sook | - |
dc.contributor.author | Kim, Myung-Suk | - |
dc.contributor.author | Park, Jong-Wan | - |
dc.date.accessioned | 2010-01-04 | - |
dc.date.available | 2010-01-04 | - |
dc.date.issued | 2006 | - |
dc.identifier.citation | Biochimie 88 (2006) 163-169 | en |
dc.identifier.issn | 0300-9084 (Print) | - |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16139409 | - |
dc.identifier.uri | https://hdl.handle.net/10371/24799 | - |
dc.description.abstract | HIF-1alpha is a transcription factor involved in the cellular adaptation to either hypoxia or iron deficiency. In the presence of oxygen and iron, proline residues in two degradation domains are modified by HIF-1-prolyl hydroxylases (PHDs), resulting in ubiquitination and degradation of HIF-1alpha. Since both molecular oxygen and iron are elements required for this hydroxylation process, HIF-1alpha might be unmodified and stable in conditions lacking oxygen or iron. If so, two degradation domains may respond to hypoxia and iron-depletion in the same way. In this study, however, we found two degradation domains to differentially regulate the stability of HIF-1alpha. The C-terminal domain responded to both hypoxia and iron-depletion, but the N-terminal domain to only iron-depletion. The deletion or point-mutation of the C-terminal domain blunted the hypoxic induction of HIF-1alpha. However, PHD-silencing siRNAs revealed that two degradation domains were not regulated by different types of PHDs. Both domains were regulated mainly by PHD2. The further mutational analysis demonstrated that the ARD1-acetylated motif near the C-terminal degradation domain (CDD) modulates the oxygen-dependent regulation of HIF-1alpha. The oxygen-dependent HIF-1alpha regulation requiring both proline hydroxylation and lysine acetylation may be more complicated than the iron-dependent regulation requiring only proline hydroxylation. | en |
dc.language.iso | en | en |
dc.publisher | Elsevier | en |
dc.subject | Anoxia/*metabolism | en |
dc.subject | Cell Line | en |
dc.subject | Deferoxamine/metabolism | en |
dc.subject | Humans | en |
dc.subject | Hypoxia-Inducible Factor 1, alpha Subunit/genetics/*metabolism | en |
dc.subject | Iron/*deficiency/metabolism | en |
dc.subject | Oxygen/*metabolism | en |
dc.subject | Point Mutation | en |
dc.subject | Protein Structure, Tertiary | en |
dc.subject | RNA, Small Interfering/genetics/metabolism | en |
dc.subject | RNA, Small Interfering/genetics/metabolism | en |
dc.title | Differential responses of two degradation domains of HIF-1alpha to hypoxia and iron deficiency | en |
dc.type | Article | en |
dc.contributor.AlternativeAuthor | 이경화 | - |
dc.contributor.AlternativeAuthor | 최은주 | - |
dc.contributor.AlternativeAuthor | 전양숙 | - |
dc.contributor.AlternativeAuthor | 김명석 | - |
dc.contributor.AlternativeAuthor | 박종완 | - |
dc.identifier.doi | 10.1016/j.biochi.2005.07.011 | - |
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