Publications
Detailed Information
STAT3 inhibits the degradation of HIF-1alpha by pVHL-mediated ubiquitination
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Jung, Joo Eun | - |
dc.contributor.author | Kim, Hong Sook | - |
dc.contributor.author | Lee, Chang Seok | - |
dc.contributor.author | Shin, Yong-Jae | - |
dc.contributor.author | Kim, Yong-Nyun | - |
dc.contributor.author | Kang, Gyeong-Hoon | - |
dc.contributor.author | Kim, Tae-You | - |
dc.contributor.author | Juhnn, Yong-Sung | - |
dc.contributor.author | Kim, Sung-Joon | - |
dc.contributor.author | Park, Jong-Wan | - |
dc.contributor.author | Ye, Sang-Kyu | - |
dc.contributor.author | Chung, Myung-Hee | - |
dc.date.accessioned | 2009-06-08T01:19:17Z | - |
dc.date.available | 2009-06-08T01:19:17Z | - |
dc.date.issued | 2008 | - |
dc.identifier.citation | Exp Mol Med 2008;40:479-85 | en |
dc.identifier.issn | 1226-3613 | - |
dc.identifier.uri | http://www.e-emm.org | - |
dc.identifier.uri | https://hdl.handle.net/10371/4441 | - |
dc.description.abstract | Hypoxia-inducible factor 1alpha (HIF-1alpha) is rapidly degraded by the ubiquitin-proteasome pathway under normoxic conditions. Ubiquitination of HIF-1alpha is mediated by interaction with von Hippel-Lindau tumor suppressor protein (pVHL). In our previous report, we found that hypoxia-induced active signal transducer and activator of transcription3 (STAT3) accelerated the accumulation of HIF-1alpha protein and prolonged its half-life in solid tumor cells. However, its specific mechanisms are not fully understood. Thus, we examined the role of STAT3 in the mechanism of pVHL-mediated HIF-1alpha stability. We found that STAT3 interacts with C-terminal domain of HIF-1alpha and stabilizes HIF-1alpha by inhibition of pVHL binding to HIF-1alpha. The binding between HIF-1alpha and pVHL, negative regulator of HIF-1alpha stability, was interfered dose-dependently by overexpressed constitutive active STAT3. Moreover, we found that the enhanced HIF-1alpha protein levels by active STAT3 are due to decrease of poly-ubiquitination of HIF-1alpha protein via inhibition of interaction between pVHL and HIF-1alpha. Taken together, our results suggest that STAT3 decreases the pVHL-mediated ubiquitination of HIF-1alpha through competition with pVHL for binding to HIF-1 alpha, and then stabilizes HIF-1alpha protein levels. | en |
dc.description.sponsorship | This work was supported by a grant from the 2007 National R&D Program for Cancer Control, Ministry of Health and Welfare (Project No.: 800-20070230), and Korean Science and Engineering Foundation (R01-2006-000-10977-0). | en |
dc.language.iso | en | - |
dc.publisher | Korean Society of Medical Biochemistry and Molecular Biology = 대한 생화학·분자생물학회 | en |
dc.subject | anoxia | en |
dc.subject | hypoxia-inducible factor1 | en |
dc.subject | α subunit | en |
dc.subject | neoplasms | en |
dc.subject | STAT3 transcription factor | en |
dc.subject | ubiquitination | en |
dc.subject | von Hippel-Lindau tumor suppressor protein | en |
dc.title | STAT3 inhibits the degradation of HIF-1alpha by pVHL-mediated ubiquitination | en |
dc.type | Article | en |
dc.contributor.AlternativeAuthor | 정주은 | - |
dc.contributor.AlternativeAuthor | 김홍숙 | - |
dc.contributor.AlternativeAuthor | 이창석 | - |
dc.contributor.AlternativeAuthor | 신용재 | - |
dc.contributor.AlternativeAuthor | 김용년 | - |
dc.contributor.AlternativeAuthor | 강경훈 | - |
dc.contributor.AlternativeAuthor | 김태유 | - |
dc.contributor.AlternativeAuthor | 전용성 | - |
dc.contributor.AlternativeAuthor | 김성준 | - |
dc.contributor.AlternativeAuthor | 박종완 | - |
dc.contributor.AlternativeAuthor | 예상규 | - |
dc.identifier.doi | 10.3858/emm.2008.40.5.479 | - |
dc.identifier.doi | 10.3858/emm.2008.40.5.479 | - |
dc.citation.journaltitle | Experimental & molecular medicine | - |
- Appears in Collections:
- Files in This Item:
Item View & Download Count
Items in S-Space are protected by copyright, with all rights reserved, unless otherwise indicated.