Abstract
The plasma membrane (PM) is frequently challenged by mechanical stresses. In budding yeast, TORC2-Ypk1/Ypk2 kinase cascade plays a crucial 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. Genetic evidence suggests that this process is mediated by the Lem3-containing lipid flippase.We propose that lipid remodeling mediated by the TORC2-Ypk1/Ypk2-Lem3 axis is a backup mechanism for PM anchoring of Rho1 after PM stressinduced acute degradation of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], which is responsible for Rho1 localization under normal conditions. Since all the signaling molecules studied here are conserved in higher eukaryotes, our findings might represent a general mechanism to cope with PM stress.
| Original language | English |
|---|---|
| Pages (from-to) | 1169-1178 |
| Number of pages | 10 |
| Journal | Journal of Cell Science |
| Volume | 130 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2017 Jan 1 |
| Externally published | Yes |
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Keywords
- Actin cytoskeleton
- Akt
- Flippase
- Membrane stress
- Phosphatidylserine
- Rho
ASJC Scopus subject areas
- Cell Biology
Cite this
Ypk1 and Ypk2 kinases maintain Rho1 at the plasma membrane by flippase-dependent lipid remodeling after membrane stresses. / Hatakeyama, Riko; Kono, Keiko; Yoshida, Satoshi.
In: Journal of Cell Science, Vol. 130, No. 6, 01.01.2017, p. 1169-1178.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Ypk1 and Ypk2 kinases maintain Rho1 at the plasma membrane by flippase-dependent lipid remodeling after membrane stresses
AU - Hatakeyama, Riko
AU - Kono, Keiko
AU - Yoshida, Satoshi
PY - 2017/1/1
Y1 - 2017/1/1
N2 - The plasma membrane (PM) is frequently challenged by mechanical stresses. In budding yeast, TORC2-Ypk1/Ypk2 kinase cascade plays a crucial 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. Genetic evidence suggests that this process is mediated by the Lem3-containing lipid flippase.We propose that lipid remodeling mediated by the TORC2-Ypk1/Ypk2-Lem3 axis is a backup mechanism for PM anchoring of Rho1 after PM stressinduced acute degradation of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], which is responsible for Rho1 localization under normal conditions. Since all the signaling molecules studied here are conserved in higher eukaryotes, our findings might represent a general mechanism to cope with PM stress.
AB - The plasma membrane (PM) is frequently challenged by mechanical stresses. In budding yeast, TORC2-Ypk1/Ypk2 kinase cascade plays a crucial 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. Genetic evidence suggests that this process is mediated by the Lem3-containing lipid flippase.We propose that lipid remodeling mediated by the TORC2-Ypk1/Ypk2-Lem3 axis is a backup mechanism for PM anchoring of Rho1 after PM stressinduced acute degradation of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], which is responsible for Rho1 localization under normal conditions. Since all the signaling molecules studied here are conserved in higher eukaryotes, our findings might represent a general mechanism to cope with PM stress.
KW - Actin cytoskeleton
KW - Akt
KW - Flippase
KW - Membrane stress
KW - Phosphatidylserine
KW - Rho
UR - http://www.scopus.com/inward/record.url?scp=85015256440&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85015256440&partnerID=8YFLogxK
U2 - 10.1242/jcs.198382
DO - 10.1242/jcs.198382
M3 - Article
C2 - 28167678
AN - SCOPUS:85015256440
VL - 130
SP - 1169
EP - 1178
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - 6
ER -