Ypk1/Ypk2 kinases maintain Rho1 at the plasma membrane by flippase-dependent lipid remodelling after membrane stresses
- Hatakeyama, Riko Department of Biology and Rosenstiel Basic Biomedical Research Center, Brandeis University, Waltham, MA, USA - Department of Biology, University of Fribourg, Switzerland
- Kono, Keiko Department of Cell Biology, Graduate School of Medical Sciences, Nagoya City University, Nagoya, Japan
- Yoshida, Satoshi Department of Biology and Rosenstiel Basic Biomedical Research Center, Brandeis University, Waltham, MA, USA - Gunma Initiative for Advanced Research (GIAR), Gunma University, Gunma, Japan - Institute for Molecular and Cellular Regulation, Gunma University, Gunma, Japan
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01.01.2017
Published in:
- J Cell Sci. - 2017, p. jcs.198382
English
The plasma membrane (PM) is frequently challenged by mechanical stresses. In budding yeast, TORC2-Ypk1/Ypk2 kinase cascade plays a critical role in PM stress responses by reorganizing the actin cytoskeleton via Rho1 GTPase. However, the molecular mechanism by which TORC2-Ypk1/Ypk2 regulates Rho1 is not well defined. Here, we found that Ypk1/Ypk2 maintain PM localization of Rho1 under PM stress via spatial reorganization of the lipids including phosphatidylserine (PS). Genetic evidence suggests that this process is mediated by the Lem3-containing lipid flippase. We propose that TORC2-Ypk1/Ypk2-Lem3 axis-mediated lipid remodelling is a backup mechanism for PM anchoring of Rho1 after PM stress-induced acute degradation of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), which is responsible for Rho1 localization in a normal condition. Since all the signaling molecules studied here are conserved in higher eukaryotes, our findings may represent a general mechanism to cope with PM stress.
- Faculty
- Faculté des sciences et de médecine
- Department
- Département de Biologie
- Language
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- English
- Classification
- Biological sciences
- License
- License undefined
- Identifiers
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- RERO DOC 279080
- DOI 10.1242/jcs.198382
- Persistent URL
- https://folia.unifr.ch/unifr/documents/305267
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