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  A Eukaryotic Sensor for Membrane Lipid Saturation

Covino, R., Ballweg, S., Stordeur, C., Michaelis, J. B., Puth, K., Wernig, F., et al. (2016). A Eukaryotic Sensor for Membrane Lipid Saturation. Molecular Cell, 63(1), 49-59. doi:10.1016/j.molcel.2016.05.015.

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 Creators:
Covino, Roberto1, Author           
Ballweg, Stephanie2, Author
Stordeur, Claudius2, Author
Michaelis, Jonas B.2, Author
Puth, Kristina2, Author
Wernig, Florian2, Author
Bahrami, Amir Houshang1, Author           
Ernst, Andreas M.3, Author
Hummer, Gerhard1, Author           
Ernst, Robert2, Author
Affiliations:
1Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
2Institute of Biochemistry and Buchmann and Institute for Molecular Life Sciences, Goethe University Frankfurt, I 60438 Frankfurt, Germany, ou_persistent22              
3Department of Cell Biology, School of Medicine, Yale University, New Haven, CT 06510, USA, ou_persistent22              

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 Abstract: Maintaining a fluid bilayer is essential for cell signaling and survival. Lipid saturation is a key factor determining lipid packing and membrane fluidity, and it must be tightly controlled to guarantee organelle function and identity. A dedicated eukaryotic mechanism of lipid saturation sensing, however, remains elusive. Here we show that Mga2, a transcription factor conserved among fungi, acts as a lipid-packing sensor in the ER membrane to control the production of unsaturated fatty acids. Systematic mutagenesis, molecular dynamics simulations, and electron paramagnetic resonance spectroscopy identify a pivotal role of the oligomeric transmembrane helix (TMH) of Mga2 for intra-membrane sensing, and they show that the lipid environment controls the proteolytic activation of Mga2 by stabilizing alternative rotational orientations of the TMH region. This work establishes a eukaryotic strategy of lipid saturation sensing that differs significantly from the analogous bacterial mechanism relying on hydrophobic thickness

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Language(s): eng - English
 Dates: 2015-12-152016-05-112016-06-162016-07-17
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.molcel.2016.05.015
 Degree: -

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Title: Molecular Cell
Source Genre: Journal
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Publ. Info: Cambridge, Mass. : Cell Press
Pages: - Volume / Issue: 63 (1) Sequence Number: - Start / End Page: 49 - 59 Identifier: ISSN: 1097-2765
CoNE: https://pure.mpg.de/cone/journals/resource/954925610929