HSF1 phosphorylation establishes an active chromatin state via the TRRAP–TIP60 complex and promotes tumorigenesis

Mitsuaki Fujimoto, Ryosuke Takii, Masaki Matsumoto, Mariko Okada, Keiich I. Nakayama, Ryuichiro Nakato, Katsunori Fujiki, Katsuhiko Shirahige and Akira Nakai ()
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Mitsuaki Fujimoto: Yamaguchi University School of Medicine
Ryosuke Takii: Yamaguchi University School of Medicine
Masaki Matsumoto: Niigata University
Mariko Okada: Yamaguchi University School of Medicine
Keiich I. Nakayama: Kyushu University
Ryuichiro Nakato: University of Tokyo
Katsunori Fujiki: University of Tokyo
Katsuhiko Shirahige: University of Tokyo
Akira Nakai: Yamaguchi University School of Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-18

Abstract: Abstract Transcriptional regulation by RNA polymerase II is associated with changes in chromatin structure. Activated and promoter-bound heat shock transcription factor 1 (HSF1) recruits transcriptional co-activators, including histone-modifying enzymes; however, the mechanisms underlying chromatin opening remain unclear. Here, we demonstrate that HSF1 recruits the TRRAP-TIP60 acetyltransferase complex in HSP72 promoter during heat shock in a manner dependent on phosphorylation of HSF1-S419. TRIM33, a bromodomain-containing ubiquitin ligase, is then recruited to the promoter by interactions with HSF1 and a TIP60-mediated acetylation mark, and cooperates with the related factor TRIM24 for mono-ubiquitination of histone H2B on K120. These changes in histone modifications are triggered by phosphorylation of HSF1-S419 via PLK1, and stabilize the HSF1-transcription complex in HSP72 promoter. Furthermore, HSF1-S419 phosphorylation is constitutively enhanced in and promotes proliferation of melanoma cells. Our results provide mechanisms for HSF1 phosphorylation-dependent establishment of an active chromatin status, which is important for tumorigenesis.

Date: 2022
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DOI: 10.1038/s41467-022-32034-4

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