Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis

Berchtold, Doris, Piccolis, Manuele, Chiaruttini, Nicolas, Riezman, Isabelle, Riezman, Howard, Roux, Aurelien, Walther, Tobias C. and Loewith, Robbie (2012) Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis. Nature Cell Biology, 14 5: 542-547. doi:10.1038/ncb2480


Author Berchtold, Doris
Piccolis, Manuele
Chiaruttini, Nicolas
Riezman, Isabelle
Riezman, Howard
Roux, Aurelien
Walther, Tobias C.
Loewith, Robbie
Title Plasma membrane stress induces relocalization of Slm proteins and activation of TORC2 to promote sphingolipid synthesis
Journal name Nature Cell Biology   Check publisher's open access policy
ISSN 1465-7392
1476-4679
Publication date 2012-05-01
Sub-type Article (original research)
DOI 10.1038/ncb2480
Volume 14
Issue 5
Start page 542
End page 547
Total pages 6
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
Abstract The plasma membrane delimits the cell, and its integrity is essential for cell survival. Lipids and proteins form domains of distinct composition within the plasma membrane. How changes in plasma membrane composition are perceived, and how the abundance of lipids in the plasma membrane is regulated to balance changing needs remains largely unknown. Here, we show that the Slm1/2 paralogues and the target of rapamycin kinase complex 2 (TORC2) play a central role in this regulation. Membrane stress, induced by either inhibition of sphingolipid metabolism or by mechanically stretching the plasma membrane, redistributes Slm proteins between distinct plasma membrane domains. This increases Slm protein association with and activation of TORC2, which is restricted to the domain known as the membrane compartment containing TORC2 (MCT; ref.1 ). As TORC2 regulates sphingolipid metabolism, our discoveries reveal a homeostasis mechanism in which TORC2 responds to plasma membrane stress to mediate compensatory changes in cellular lipid synthesis and hence modulates the composition of the plasma membrane. The components of this pathway and their involvement in signalling after membrane stretch are evolutionarily conserved.
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status Non-UQ
Additional Notes Published under Letters

Document type: Journal Article
Sub-type: Article (original research)
Collections: Non HERDC
Institute for Molecular Bioscience - Publications
 
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Created: Mon, 10 Sep 2012, 19:30:33 EST by Susan Allen on behalf of Institute for Molecular Bioscience