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首页> 外文期刊>Molecular and Cellular Biology >Heat Shock-Induced SRSF10 Dephosphorylation Displays Thermotolerance Mediated by Hsp27
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Heat Shock-Induced SRSF10 Dephosphorylation Displays Thermotolerance Mediated by Hsp27

机译：热激诱导的SRSF10去磷酸化显示由Hsp27介导的耐热性

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Gene regulation in response to environmental stress is critical for the survival of all organisms. From Saccharomyces cerevisiae to humans, it has been observed that splicing of mRNA precursors is repressed upon heat shock. However, a mild heat pretreatment often prevents splicing inhibition in response to a subsequent and more severe heat shock, a phenomenon called splicing thermotolerance. We have shown previously that the splicing regulator SRSF10 (formerly SRp38) is specifically dephosphorylated by the phosphatase PP1 in response to heat shock and that dephosphorylated SRSF10 is responsible for splicing repression caused by heat shock. Here we report that a mild heat shock protects SRSF10 from dephosphorylation during a second and more severe heat shock. Furthermore, this “thermotolerance” of SRSF10 phosphorylation, like that of splicing, requires de novo protein synthesis, specifically the synthesis of heat shock proteins. Indeed, overexpression of one of these proteins, Hsp27, inhibits SRSF10 dephosphorylation in response to heat shock and does so by interaction with SRSF10. Our data thus provide evidence that splicing thermotolerance is acquired through maintenance of SRSF10 phosphorylation and that this is mediated at least in part by Hsp27.
机译：响应环境压力的基因调控对于所有生物的生存至关重要。从酿酒酵母到人类，已经发现在热激后，mRNA前体的剪接受到抑制。但是，温和的热处理通常会阻止对随后的更严重的热冲击的熔接抑制，这种现象称为熔接耐热性。先前我们已经表明，剪接调节剂SRSF10（以前称为SRp38）是由磷酸酶PP1响应热冲击而特异性去磷酸化的，而去磷酸化的SRSF10则是由热冲击引起的剪接抑制的原因。在这里，我们报告，在第二次或更严重的热冲击过程中，轻度的热冲击可保护SRSF10免受脱磷酸作用。此外，像剪接一样，SRSF10磷酸化的这种“耐热性”要求从头合成蛋白质，特别是热激蛋白。实际上，这些蛋白之一Hsp27的过表达会抑制SRSF10响应热激而去磷酸化，并通过与SRSF10相互作用来抑制。因此，我们的数据提供了通过维持SRSF10磷酸化获得拼接耐热性的证据，并且该耐热性至少部分地由Hsp27介导。

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