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Membrane-mediated protein interactions drive membrane protein organization

The plasma membrane’s main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the...

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Autores principales: Jiang, Yining, Thienpont, Batiste, Sapuru, Vinay, Hite, Richard K., Dittman, Jeremy S., Sturgis, James N., Scheuring, Simon
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9712761/
https://www.ncbi.nlm.nih.gov/pubmed/36450733
http://dx.doi.org/10.1038/s41467-022-35202-8
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author Jiang, Yining
Thienpont, Batiste
Sapuru, Vinay
Hite, Richard K.
Dittman, Jeremy S.
Sturgis, James N.
Scheuring, Simon
author_facet Jiang, Yining
Thienpont, Batiste
Sapuru, Vinay
Hite, Richard K.
Dittman, Jeremy S.
Sturgis, James N.
Scheuring, Simon
author_sort Jiang, Yining
collection PubMed
description The plasma membrane’s main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the biophysical determinants of membrane-mediated protein interactions must be considered to understand membrane protein organization. Here, we used high-speed atomic force microscopy and kinetic and membrane elastic theory to investigate the behavior of a model membrane protein in oligomerization and assembly in controlled lipid environments. We find that membrane hydrophobic mismatch modulates oligomerization and assembly energetics, and 2D organization. Our experimental and theoretical frameworks reveal how membrane organization can emerge from Brownian diffusion and a minimal set of physical properties of the membrane constituents.
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spelling pubmed-97127612022-12-02 Membrane-mediated protein interactions drive membrane protein organization Jiang, Yining Thienpont, Batiste Sapuru, Vinay Hite, Richard K. Dittman, Jeremy S. Sturgis, James N. Scheuring, Simon Nat Commun Article The plasma membrane’s main constituents, i.e., phospholipids and membrane proteins, are known to be organized in lipid-protein functional domains and supercomplexes. No active membrane-intrinsic process is known to establish membrane organization. Thus, the interplay of thermal fluctuations and the biophysical determinants of membrane-mediated protein interactions must be considered to understand membrane protein organization. Here, we used high-speed atomic force microscopy and kinetic and membrane elastic theory to investigate the behavior of a model membrane protein in oligomerization and assembly in controlled lipid environments. We find that membrane hydrophobic mismatch modulates oligomerization and assembly energetics, and 2D organization. Our experimental and theoretical frameworks reveal how membrane organization can emerge from Brownian diffusion and a minimal set of physical properties of the membrane constituents. Nature Publishing Group UK 2022-11-30 /pmc/articles/PMC9712761/ /pubmed/36450733 http://dx.doi.org/10.1038/s41467-022-35202-8 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Jiang, Yining
Thienpont, Batiste
Sapuru, Vinay
Hite, Richard K.
Dittman, Jeremy S.
Sturgis, James N.
Scheuring, Simon
Membrane-mediated protein interactions drive membrane protein organization
title Membrane-mediated protein interactions drive membrane protein organization
title_full Membrane-mediated protein interactions drive membrane protein organization
title_fullStr Membrane-mediated protein interactions drive membrane protein organization
title_full_unstemmed Membrane-mediated protein interactions drive membrane protein organization
title_short Membrane-mediated protein interactions drive membrane protein organization
title_sort membrane-mediated protein interactions drive membrane protein organization
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9712761/
https://www.ncbi.nlm.nih.gov/pubmed/36450733
http://dx.doi.org/10.1038/s41467-022-35202-8
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