ArticleMolecular and cellular biology2011
Heat shock-induced SRSF10 dephosphorylation displays thermotolerance mediated by Hsp27.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- SRSF10: an atypical splicing regulator with critical roles in stress response, organ development, and viral replication.RNA (New York, N.Y.) · 2021Review
- Identification of SRSF10 as a regulator of SMN2 ISS-N1.Human mutation · 2021Article
- Global Transcriptomics Uncovers Distinct Contributions From Splicing Regulatory Proteins to the Macrophage Innate Immune Response.Frontiers in immunology · 2021Article
- HSP27 is a partner of JAK2-STAT5 and a potential therapeutic target in myelofibrosis.Nature communications · 2018Article
- AyurvedicJournal of biosciences · 2016Article
- New levels of transcriptome complexity at upper thermal limits in wild Drosophila revealed by exon expression analysis.Genetics · 2013Article
- Review
- Regulation of survival gene hsp70.Cell stress & chaperones · 2012Review
- The RNAissance family: SR proteins as multifaceted regulators of gene expression.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.