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Decrease in plasma membrane tension triggers PtdIns(4,5)P2 phase separation to inactivate TORC2

delete2018-08-27
delete107
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OA
AI
M
Margot Riggi
K
Karolina Niewola‐Staszkowska
N
Nicolas Chiaruttini
A
Adai Colom
B
Beata Kuśmider
V
Vincent Mercier
S
Saeideh Soleimanpour
M
Michael Ståhl
S
Stefan Matile
A
Aurélien Roux *
R
Robbie Loewith *
DOI:10.1038/s41556-018-0150-zdelete
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摘要

摘要

En 中文
The target of rapamycin complex 2 (TORC2) plays a key role in maintaining the homeostasis of plasma membrane (PM) tension. TORC2 activation following increased PM tension involves redistribution of the Slm1 and 2 paralogues from PM invaginations known as eisosomes into membrane compartments containing TORC2. How Slm1/2 relocalization is triggered, and if/how this plays a role in TORC2 inactivation with decreased PM tension, is unknown. Using osmotic shocks and palmitoylcarnitine as orthogonal tools to manipulate PM tension, we demonstrate that decreased PM tension triggers spontaneous, energy-independent reorganization of pre-existing phosphatidylinositol-4,5-bisphosphate into discrete invaginated membrane domains, which cluster and inactivate TORC2. These results demonstrate that increased and decreased membrane tension are sensed through different mechanisms, highlighting a role for membrane lipid phase separation in mechanotransduction.
Keyword:
PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE CLUSTERS
RAPAMYCIN COMPLEX 2
SACCHAROMYCES-CEREVISIAE
ACTIN CYTOSKELETON
PROTEINS SLM1
CELL-SHAPE
YEAST
POLARIZATION
TARGET
ENDOCYTOSIS
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期刊

Nature Cell Biology 封面图
Nature Cell Biology
IF:
19.1
论文数:
6.2K
被引数:
4.8W

机构

U
university of geneva
学者数:
3.6W
论文数: 2.9W
被引数: 35
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