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Calcineurin phosphatase in signal transduction: lessons from fission yeast
Author(s) -
Sugiura Reiko,
Sio Susie O.,
Shuntoh Hisato,
Kuno Takayoshi
Publication year - 2002
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1046/j.1365-2443.2002.00557.x
Subject(s) - calcineurin , biology , phosphatase , signal transduction , schizosaccharomyces pombe , gtpase , microbiology and biotechnology , biochemistry , yeast , phosphorylation , saccharomyces cerevisiae , medicine , surgery , transplantation
Calcineurin (protein phosphatase 2B), the only serine/threonine phosphatase under the control of Ca 2+ /calmodulin, is an important mediator in signal transmission, connecting the Ca 2+ ‐dependent signalling to a wide variety of cellular responses. Furthermore, calcineurin is specifically inhibited by the immunosuppressant drugs cyclosporin A and tacrolimus (FK506), and these drugs have been a powerful tool for identifying many of the roles of calcineurin. Calcineurin is enriched in the neural tissues, and also distributes broadly in other tissues. The structure of the protein is highly conserved from yeast to man. The combined use of powerful genetics and of specific calcineurin inhibitors in fission yeast Schizosaccharomyces pombe ( S. pombe ) identified new components of the calcineurin pathway, and defined new roles of calcineurin in the regulation of the many cellular processes. Recent data has revealed functional interactions in which calcineurin phosphatase is involved, such as the cross‐talk between the Pmk1 MAP kinase signalling, or the PI signalling. Calcineurin also participates in membrane traffic and cytokinesis of fission yeast through its functional connection with members of the small GTPase Rab/Ypt family, and Type II myosin, respectively. These findings highlight the potential of fission yeast genetic studies to elucidate conserved elements of signal transduction cascades.