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Acta Biochim Biophys Sin (Shanghai). 2014 Feb;46(2):136-40. doi: 10.1093/abbs/gmt136. Epub 2013 Dec 26.

RNF20 promotes the polyubiquitination and proteasome-dependent degradation of AP-2α protein.

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1
Key Laboratory of Protein Chemistry and Developmental Biology of Ministry of Education, College of Life Science, Hunan Normal University, Changsha 410081, China.

Abstract

Transcription factor activator protein 2α (AP-2α) is a negative regulator of adipogenesis by repressing the transcription of CCAAT/enhancer binding protein (C/EBPα) gene. During adipogenesis, AP-2α is degraded, leading to transcriptional up-regulation of C/EBPα. However, the mechanism for AP-2α degradation is not clear. Here, using immunoprecipitation assay and mass spectrometry, we identified ring finger protein 20 (RNF20) as an AP-2α-interacting protein in 3T3-L1 preadipocytes. RNF20 has been proved to be an E3 ubiquitin ligase for both histone H2B and tumor suppressor ErbB3-binding protein 1 (Ebp1). In this study, we demonstrated that RNF20 co-localized and interacted with AP-2α, and promoted its polyubiquitination and proteasome-dependent degradation. Over-expression of RNF20 inhibited the activity of AP-2α and rescued the C/EBPα expression which was inhibited by AP-2α. These results suggested that RNF20 may play roles in adipocyte differentiation by stimulating ubiquitin-proteasome-dependent degradation of AP-2α.

KEYWORDS:

AP-2α; C/EBPα; E3 ubiquitin ligase; RNF20; ubiquitin–proteasome-dependent degradation

PMID:
24374663
DOI:
10.1093/abbs/gmt136
[Indexed for MEDLINE]
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