Cited by 289Signaling Pathways in DiseaseFungal and yeast genetics researchProtein Tyrosine Phosphatases

Yeast has homologs (CNA1 and CNA2 gene products) of mammalian calcineurin, a calmodulin-regulated phosphoprotein phosphatase

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Cyert, M S, Kunisawa, R, Kaim, D, Thorner, J·1991·Proceedings of the National Academy of Sciences

Abstract

Calcineurin, or phosphoprotein phosphatase type 2B (PP2B), is a calmodulin-regulated phosphoprotein phosphatase. We isolated a gene encoding a yeast PP2B homolog (CNA1) by screening a yeast genomic DNA library in the expression vector lambda gt11, first with 125I-labeled yeast calmodulin and then with a human cDNA encoding the catalytic (or A) subunit of calcineurin. The predicted CNA1 gene product is 54% identical to its mammalian counterpart. Using the polymerase chain reaction (PCR) with oligonucleotide primers based on sequences conserved between CNA1 and mammalian PP2B genes, we isolated a second gene, CNA2. CNA2 is identical to PP2Bw, a partial cDNA clone previously described by others as originating from rabbit brain tissue. Our findings demonstrate that a unicellular eukaryote contains phosphoprotein phosphatases of the 2B class. Haploid cells containing a single cna1 or cna2 null mutation, or both mutations, were viable. MATa cna1 cna2 double mutants were more sensitive than wild-type cells or either single mutant to growth arrest induced by the mating pheromone alpha factor and failed to resume growth during continuous exposure to alpha factor. Thus, calcineurin action antagonizes the mating-pheromone response pathway.

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Crossref · 10.1073/pnas.88.16.7376

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  • Calcineurin is required in S. cerevisiae and S. pombe for adaptation to environmental stresses, cation homeostasis, morphogenesis, cell wall integrity, and mating.

    “Calcineurin has been well characterized in the model yeasts S. cerevisiae and Schizosaccharomyces pombe, where it is required for adaptation to a variety of environmental stresses, cation homeostasis, morphogenesis, cell wall integrity, and mating (Cyert et al., 1991; Matsumoto et al., 2002; Mendoza et al., 1996; Mendoza et al., 1994; Sugiura et al., 2002).”

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Authors
Cyert, M. S., Kunisawa, R., Kaim, D., & Thorner, J.
Affiliations
University of California, Berkeley (US)
Venue
Proceedings of the National Academy of Sciences
Published
1991-08-15
Volume
88
Issue
16
Pages
7376-7380
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1985339191
Cited by
289
References
49
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 5 · 2019: 6 · 2018: 2 · 2017: 1 · 2016: 4 · 2015: 5 · 2014: 7 · 2013: 5 · 2012: 6
FWCI
9.65
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • American Cancer Society
  • Life Sciences Research Foundation
  • National Institutes of Health (GM21841)
  • National Institute of General Medical Sciences (GM 21841)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
calcineurin, yeast, calmodulin, mating pheromone response, alpha-factor, knockout mutants, gene cloning, homologous genes
MeSH terms
Amino Acid Sequence, Animals, Calcium-Binding Proteins, Calmodulin-Binding Proteins, Cloning, Molecular, DNA, Fungal, Genes, Fungal, Molecular Sequence Data, Nucleic Acid Hybridization, Phosphoprotein Phosphatases, Rabbits, Saccharomyces cerevisiae, Sequence Homology, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Calcineurin, Saccharomyces cerevisiae Proteins, Mice

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