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MBC in Press, published online ahead of print August 23, 2006
Mol. Biol. Cell 10.1091/mbc.E06-06-0526

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Submitted on June 19, 2006
Accepted on August 15, 2006

Real-Time Monitoring of Calcineurin Activity in Living Cells: Evidence for Two Distinct Ca2+-dependent Pathways in Fission Yeast

Lu Deng,* Reiko Sugiura,*{dagger} Mai Takeuchi,* Masahiro Suzuki,* Hidemine Ebina,* Tomonori Takami,* Atsushi Koike,* Shiori Iba,* and Takayoshi Kuno*

*Division of Molecular Pharmacology and Pharmacogenomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan; {dagger}Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, Kowakae 3-4-1, Higashi-Osaka, 577-8502, Japan

Monitoring Editor: Fred Chang

In fission yeast, calcineurin dephosphorylates and activates the Prz1 transcription factor. Here, we identified the calcineurin-dependent response element (CDRE) in the promoter region of prz1+ gene, and monitored the calcineurin activity in living cells using a destabilized luciferase reporter gene fused to three tandem repeats of CDRE. Elevated extracellular CaCl2 caused an increase in calcineurin activity with an initial peak, and then approached a sustained constant level in a concentration-dependent manner. In CaCl2-sensitive mutants such as {Delta}pmc1, the response was markedly enhanced reflecting its high intracellular Ca2+. Agents expected to induce Ca2+ influx showed distinct patterns of the CDRE-reporter activity suggesting different mechanisms of calcineurin activation. Knockout of yam8+ or cch1+ encoding putative subunits of a Ca2+ channel abolished the activation of calcineurin upon exposure to various stimuli including high extracellular NaCl and cell wall-damaging agents. However, knockout of yam8+ or cch1+ did not affect the activation of calcineurin upon stimulation by elevated extracellular Ca2+. The Pck2 protein kinase C-Pmk1 MAP kinase pathway was required for the stimulation of calcineurin via Yam8/Cch1 mediated Ca2+ influx, but it was not required for the stimulation by elevated extracellular Ca2+, suggesting two distinct pathways for calcineurin activation.

Address correspondence to: Takayoshi Kuno (tkuno{at}med.kobe-u.ac.jp)




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