Early protection to stress mediated by CDK-dependent PI3,5P2 signaling from the vacuole/lysosome.

Adaptation to environmental stress is critical for cell survival. Adaptation generally occurs via changes in transcription and translation. However, there is a time lag before changes in gene expression, which suggests that more rapid mechanisms likely exist. In this study, we show that in yeast, the cyclin-dependent kinase Pho85/CDK5 provides ...
protection against hyperosmotic stress and acts before long-term adaptation provided by Hog1. This protection requires the vacuolar/endolysosomal signaling lipid PI3,5P2 We show that Pho85/CDK5 directly phosphorylates and positively regulates the PI3P-5 kinase Fab1/PIKfyve complex and provide evidence that this regulation is conserved in mammalian cells. Moreover, this regulation is particularly crucial in yeast for the stress-induced transient elevation of PI3,5P2 Our study reveals a rapid protection mechanism regulated by Pho85/CDK5 via signaling from the vacuole/lysosome, which is distinct temporally and spatially from the previously discovered long-term adaptation Hog1 pathway, which signals from the nucleus.
Mesh Terms:
Adaptation, Physiological, Animals, Cells, Cultured, Cyclin-Dependent Kinase 5, Cyclin-Dependent Kinases, Cyclins, Endosomes, Fibroblasts, Humans, Lysosomes, Membrane Proteins, Mice, Microbial Viability, Mitogen-Activated Protein Kinases, Mutation, Osmotic Pressure, Phosphatidylinositol 3-Kinases, Phosphatidylinositol Phosphates, Phosphorylation, Phosphotransferases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Second Messenger Systems, Time Factors, Up-Regulation, Vacuoles
J. Cell Biol.
Date: Jul. 03, 2017
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