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A ceramide-activated protein phosphatase mediates ceramide-induced G(1) arrest of Saccharomyces cerevisiae
Journal article   Open access   Peer reviewed

A ceramide-activated protein phosphatase mediates ceramide-induced G(1) arrest of Saccharomyces cerevisiae

J T Nickels and Broach
Genes & development, v 10(4), pp 382-394
15 Feb 1996
PMID: 8600023
url
https://doi.org/10.1101/gad.10.4.382View
Published, Version of Record (VoR) Open

Abstract

Cell Biology Developmental Biology Genetics & Heredity Life Sciences & Biomedicine Science & Technology
Certain mammalian growth modulators, such as tumor necrosis factor alpha, interleukin-1 beta, and gamma-interferon, induce an antiproliferative response-terminal differentiation, apoptosisis, or cell cycle arrest-through a novel signal transduction pathway mediated by the lipid ceramide as a second messenger. Both a ceramide-activated protein phosphatase and a ceramide-activated protein kinase have been implicated in transmitting the signals elicited by ceramide. We have determined that ceramide addition to the yeast Saccharomyces causes a similar antiproliferative response, resulting in arrest of cells in the G(1) phase of the cell cycle. We have also determined that yeast cells contain a ceramide-activated protein phosphatase composed of regulatory subunits encoded by TPD3 and CDC55 and a catalytic subunit encoded by SIT4. Because mutation of any one of these three genes renders strains resistant to ceramide inhibition, we conclude that the G(1) effects of ceramide are mediated at least in part by the yeast ceramide-activated protein phosphatase. These results highlight the conservation of signaling systems in yeast and mammalian cells and provide a novel approach to dissecting this ubiquitous signal transduction pathway.

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Web of Science research areas
Cell Biology
Developmental Biology
Genetics & Heredity
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