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Updated: Apr 19, 2026

Standardized Methods for Measuring Induction of the Heat Shock Response in Caenorhabditis elegans
Published on: July 3, 2020
Spatial control of calcineurin in response to heat shock in fission yeast
Mari Higa1, Ayako Kita, Kanako Hagihara
1Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, 3-4-1 Kowakae, Higashi-Osaka, Osaka, 577-8502, Japan.
Abstract:
In fission yeast, Ppb1, the Ca2+/calmodulin-dependent protein phosphatase calcineurin regulates multiple biological processes, such as cytokinesis, Ca2+-homeostasis, membrane trafficking and cell wall integrity. Calcineurin dephosphorylates the Prz1 transcription factor, leading to its nuclear translocation and gene expression under the control of CDRE (calcineurin-dependent response element). Although the calcineurin-mediated spatial control of downstream transcription factors has been intensively studied in many organisms, less is known about the spatial regulation of calcineurin on stresses. Here, we show that heat shock stimulates calcineurin-dependent nuclear translocation of Prz1 and CDRE-dependent gene expression. Notably, calcineurin exhibited a dramatic change in subcellular localization, translocating from diffuse cytoplasmic to dot-like structures on heat shock. The calcineurin dots colocalized with Dcp2 or Pabp, the constituent of P-bodies or stress granules, respectively, thus suggesting that calcineurin is a component of RNA granules under heat shock. Importantly, the calcineurin inhibitor FK506 markedly inhibited the accumulation of calcineurin granules, whereas the constitutively active calcineurin strongly accumulated in the granules on heat shock, suggesting that phosphatase activity is important for calcineurin localization. Notably, the depletion of calcineurin induced a rapid appearance of Nrd1- and Pabp-positive RNA granules. The possible roles of calcineurin in response to heat shock will be discussed.
Insights
Heat shock triggers calcineurin
Area of Science:
- Cell Biology
- Molecular Biology
- Stress Response
Background:
- Calcineurin (PPb1) is a Ca2+/calmodulin-dependent protein phosphatase regulating key cellular processes in fission yeast.
- Calcineurin dephosphorylates transcription factor Prz1, promoting its nuclear translocation and CDRE-dependent gene expression.
- The spatial regulation of calcineurin under stress conditions remains largely uncharacterized.
Purpose of the Study:
- To investigate the spatial regulation of calcineurin in response to heat shock in fission yeast.
- To elucidate the role of calcineurin's phosphatase activity in its stress-induced localization.
- To explore the connection between calcineurin and RNA granules during heat stress.
Main Methods:
- Microscopy to observe subcellular localization of calcineurin.
- Analysis of Prz1 nuclear translocation and CDRE-dependent gene expression.
- Investigating calcineurin localization in the presence of inhibitors (FK506) and constitutively active forms.
- Depletion studies of calcineurin and observation of RNA granule formation.
Main Results:
- Heat shock induces calcineurin-dependent nuclear translocation of Prz1 and CDRE gene expression.
- Calcineurin relocalizes from diffuse cytoplasmic distribution to dot-like structures (RNA granules) upon heat shock.
- Calcineurin's phosphatase activity is crucial for its granule localization.
- Calcineurin depletion leads to the rapid formation of RNA granules.
Conclusions:
- Calcineurin dynamically regulates gene expression in response to heat shock by altering its subcellular localization.
- Calcineurin is a component of RNA granules during heat stress, and its phosphatase activity is essential for this localization.
- These findings reveal a novel role for calcineurin in cellular stress response pathways involving RNA granules.
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