期刊
EMBO JOURNAL
卷 28, 期 22, 页码 3534-3548出版社
WILEY
DOI: 10.1038/emboj.2009.279
关键词
heat shock; PARP-1; SUMO
资金
- EEC
- La Ligue Nationale Contre le Cancer (Equipe Labellisee)
- l'Agence Nationale pour la Recherche
- Ecole Normale Superieure de Lyon
- Pasteur-Weizman Foundation
- INSERM
- Association pour la Recherche sur le Cancer
- Association for International Cancer Research
- Fondation pour la Recherche Medicale
Heat shock and other environmental stresses rapidly induce transcriptional responses subject to regulation by a variety of post-translational modifications. Among these, poly(ADP-ribosyl)ation and sumoylation have received growing attention. Here we show that the SUMO E3 ligase PIASy interacts with the poly(ADP-ribose) polymerase PARP-1, and that PIASy mediates heat shock-induced poly-sumoylation of PARP-1. Furthermore, PIASy, and hence sumoylation, appears indispensable for full activation of the inducible HSP70.1 gene. Chromatin immunoprecipitation experiments show that PIASy, SUMO and the SUMO-conjugating enzyme Ubc9 are rapidly recruited to the HSP70.1 promoter upon heat shock, and that they are subsequently released with kinetics similar to PARP-1. Finally, we provide evidence that the SUMO-targeted ubiquitin ligase RNF4 mediates heat-shock-inducible ubiquitination of PARP-1, regulates the stability of PARP-1, and, like PIASy, is a positive regulator of HSP70.1 gene activity. These results, thus, point to a novel mechanism for regulating PARP-1 transcription function, and suggest crosstalk between sumoylation and RNF4-mediated ubiquitination in regulating gene expression in response to heat shock. The EMBO Journal (2009) 28, 3534-3548. doi:10.1038/emboj.2009.279; Published online 24 September 2009
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