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Yeast calcineurin regulates nuclear localization of the Crz1p transcription factor through dephosphorylation

A Stathopoulos-Gerontides1, J J Guo, M S Cyert

  • 1Deptartment of Biological Sciences, Stanford University, Stanford, California 94305-5020 USA.

Genes & Development
|April 10, 1999
PubMed

Insights

Calcineurin signaling in yeast dephosphorylates the Crz1p transcription factor, causing its nuclear translocation. This conserved mechanism highlights shared Ca2+/calcineurin signaling pathways between yeast and mammals.

Area of Science:

  • Cellular biology
  • Molecular biology
  • Biochemistry

Background:

  • Calcineurin is a crucial Ca2+/calmodulin-dependent protein phosphatase regulating cellular processes.
  • In yeast (Saccharomyces cerevisiae), calcineurin controls Ca2+-dependent gene expression via the Crz1p transcription factor.

Purpose of the Study:

  • To investigate the mechanism by which calcineurin regulates Crz1p.
  • To identify conserved signaling pathways between yeast and mammals.

Main Methods:

  • Dephosphorylation assays to study Crz1p modification by calcineurin.
  • Localization studies to track Crz1p translocation.
  • Sequence analysis to compare Crz1p with mammalian transcription factors.

Main Results:

  • Calcineurin directly dephosphorylates Crz1p.
  • Dephosphorylation triggers Crz1p translocation to the nucleus.
  • A specific region of Crz1p is essential for calcineurin-mediated regulation.
  • This region shows similarity to mammalian NF-AT transcription factors.

Conclusions:

  • The Ca2+/calcineurin-Crz1p signaling pathway in yeast is conserved in mammalian cells.
  • This conservation extends to the regulation of transcription factor localization by calcineurin.
  • Findings reveal a fundamental mechanism of calcium signaling across eukaryotes.

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