Hip2 interacts with cyclin B1 and promotes its degradation through the ubiquitin proteasome pathway
- Authors
- Bae, Yoonhee; Choi, Dongwon; Rhim, Hyangshuk; Kang, Seongman
- Issue Date
- 19-11월-2010
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Hip2; Cyclin B1; Ubiquitination; Apoptosis
- Citation
- FEBS LETTERS, v.584, no.22, pp.4505 - 4510
- Indexed
- SCIE
SCOPUS
- Journal Title
- FEBS LETTERS
- Volume
- 584
- Number
- 22
- Start Page
- 4505
- End Page
- 4510
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/115317
- DOI
- 10.1016/j.febslet.2010.10.016
- ISSN
- 0014-5793
- Abstract
- Hip2, a ubiquitin conjugating enzyme, is involved in the suppression of cell death. The present study revealed that Hip2 regulates the stability of the apoptotic and cell cycle regulator cyclin B1. Hip2 was found to interact with cyclin B1 to promote its degradation through the ubiquitin proteasome pathway. As a result, Hip2 significantly blocked cell death induced by the cyclin B1 protein, suggesting that Hip2 is involved in the regulation of cyclin B1-mediated cell death. Structured summary: MINT-8045218, MINT-8045231: Hip2 (uniprotkb:P61086) physically interacts (MI:0915) with cyclin-B1 (uniprotkb:P14635) by pull down (MI: 0096) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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Collections - Graduate School > Department of Life Sciences > 1. Journal Articles
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