RNF20/40-mediated eEF1BL monoubiquitylation stimulates transcription of heat shock-responsive genes

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RNF20/40 E3 ubiquitin ligase-mediated histone H2B monoubiquitylation plays important roles in many cellular processes, including transcriptional regulation. However, the multiple defects observed in RNF20-depleted cells suggest additional ubiquitylation targets of RNF20/40 beyond histone H2B. Here, using biochemically defined assays employing purified factors and cell-based analyses, we demonstrate that RNF20/40, in conjunction with its cognate E2 ubiquitin-conjugating enzyme RAD6, monoubiquitylates lysine 381 of eEF1BL, a heat shock transcription factor. Notably, monoubiquitylation of eEF1BL increases eEF1BL accumulation and potentiates recruitment of p-TEFb to the promoter regions of heat shock-responsive genes, leading to enhanced transcription of these genes. We further demonstrate that cooperative physical interactions among eEF1BL, RNF20/40, and HSF1 synergistically promote expression of heat shock-responsive genes. In addition to identifying eEF1BL as a novel ubiquitylation target of RNF20/40 and elucidating its function, we provide a molecular mechanism for the cooperative function of distinct transcription factors in heat shock-responsive gene transcription.
Publisher
OXFORD UNIV PRESS
Issue Date
2019-04
Language
English
Article Type
Article
Citation

NUCLEIC ACIDS RESEARCH, v.47, no.6, pp.2840 - 2855

ISSN
0305-1048
DOI
10.1093/nar/gkz006
URI
http://hdl.handle.net/10203/262415
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
2019 In & Kim_NAR.pdf(6.7 MB)Download
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