期刊
EXPERIMENTAL CELL RESEARCH
卷 386, 期 1, 页码 -出版社
ELSEVIER INC
DOI: 10.1016/j.yexcr.2019.111686
关键词
Nuclear localization signal; Importin; HSF1; IER5; Post-translational modification; PP2A; Cancer
资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan, Institute of Chemical and Physical Research Pioneering research project [17K10261, 15K07064, 18K06235, 171103587, 18H02442, 15H05929, 19K16732]
- Applied Research for Innovative Treatment of Cancer from the Ministry of Health, Labour and Welfare
- Project for Development of Innovative Research on Cancer Therapeutics (P-Direct) from Japan Agency for Medical Research and Development
- Project for Cancer Research and Therapeutic Evolution (P-Create) from Japan Agency for Medical Research and Development
- Princess Takamatsu Cancer Research Fund
- Mitsubishi Foundation
- Novartis Foundation for the Promotion of Science
- Takeda Science Foundation
- Grants-in-Aid for Scientific Research [19K16732, 15H05929, 17K10261, 15K07064, 18K06235, 18H02442] Funding Source: KAKEN
IER5 gene encodes an activator of HSF1 and is a p53 target gene. The IER5 protein forms a ternary complex with HSF1 and PP2A, and promotes PP2A-dependent dephosphorylation of HSF1 at a number of serine and threonine residues. This hypo-phosphorylated form of HSF1 is transcriptionally active and has been suggested to be responsible for the HSF1 activation observed in cancers. Here we report that IER5 possess a classical bipartite nuclear localization signal (NLS) at amino acids 217-244 that is highly conserved among species and that mediates complex formation with importin-alpha and importin-beta. We also demonstrate that the intact NIS is essential for HSF1 dephosphorylation and full activation by IER5. Thus, nuclear import of IER5 via importin-alpha and importin-beta may be essential for IER5 function.
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