SIRT1 suppresses cellular accumulation of beta-TrCP E3 ligase via protein degradation
- Authors
- Woo, Seon Rang; Byun, Jae Gwang; Kim, Yang Hyun; Park, Eun-Ran; Joo, Hyun-Yoo; Yun, Miyong; Shin, Hyun-Jin; Kim, Su-Hyeon; Shen, Yan Nan; Park, Jeong-Eun; Park, Gil-Hong; Lee, Kee-Ho
- Issue Date
- 29-11월-2013
- Publisher
- ACADEMIC PRESS INC ELSEVIER SCIENCE
- Keywords
- beta-TrCP; SIRT1; Post-translational degradation; Pyruvate; Resveratrol; Nucleus
- Citation
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.441, no.4, pp.831 - 837
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Volume
- 441
- Number
- 4
- Start Page
- 831
- End Page
- 837
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/101553
- DOI
- 10.1016/j.bbrc.2013.10.146
- ISSN
- 0006-291X
- Abstract
- beta-Transducin repeat-containing protein (beta-TrCP), an E3 ligase, promotes the degradation of substrate proteins in response to various stimuli. Even though several beta-TrCP substrates have been identified to date, limited information of its upstream regulators is available. Here, we showed that SIRT1 suppresses beta-TrCP protein synthesis via post-translational degradation. SIRT1 depletion led to a significant increase in the beta-TrCP accumulation without affecting the mRNA level. Consistently, beta-TrCP protein accumulation induced by resveratrol was further enhanced upon SIRT1 depletion. Rescue of SIRT1 reversed the effect of resveratrol, leading to reduced beta-TrCP protein levels. Proteasomal inhibition led to recovery of beta-TrCP in cells with SIRT1 overexpression. Notably, the recovered beta-TrCP colocalized mostly with SIRT1. Thus, SIRT1 acts as a negative regulator of beta-TrCP synthesis via promoting protein degradation. (C) 2013 Elsevier Inc. All rights reserved.
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Collections - College of Medicine > Department of Medical Science > 1. Journal Articles
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