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Protein induced lipid demixing in homogeneous membranes

Bernd Henning Stumpf1, Piotr Nowakowski2,3, Christian Eggeling4,5,6, Anna Maciołek2,7, and Ana-Sunčana Smith1,8,*

  • 1PULS Group, Institut für Theoretische Physik, IZNF, Friedrich-Alexander-Universität Erlangen-Nürnberg, Cauerstraße 3, 91058 Erlangen, Germany
  • 2Max-Planck-Institut für Intelligente Systeme Stuttgart, Heisenbergstrasse 3, 70569 Stuttgart, Germany
  • 3Institut für Theoretische Physik IV, Universität Stuttgart, Pfaffenwaldring 57, 70569 Stuttgart, Germany
  • 4Institute of Applied Optics and Biophysics, Friedrich-Schiller-University Jena, 07743 Jena, Germany
  • 5Leibniz Institute of Photonic Technology e.V., 07745 Jena, Germany
  • 6MRC Human Immunology Unit and Wolfson Imaging Centre Oxford, MRC Weatherall Institute of Molecular Medicine, University of Oxford, Oxford OX3 9DS, United Kingdom
  • 7Institute of Physical Chemistry, Polish Academy of Sciences, Kasprzaka 44/52, PL-01-224 Warsaw, Poland
  • 8Group for Computational Life Sciences, Division of Physical Chemistry, Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia

  • *Corresponding author: smith@physik.fau.de

Phys. Rev. Research 3, L042013 – Published 29 October, 2021

DOI: https://doi.org/10.1103/PhysRevResearch.3.L042013

Abstract

Specific lipid environments are necessary for the establishment of protein signaling platforms in membranes, yet their origin has been highly debated. We present a continuum, exactly solvable model of protein induced local demixing of lipid membranes. The coupling between a local composition and a local thickness of the membrane induces lipid domains around inclusions with hydrophobic mismatch, even for temperatures above the miscibility critical point of the membrane. The model qualitatively explains the experimentally observed formation of lipid domains induced by anchoring of reconstituted actin in flat supported lipid bilayers.

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References (48)

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