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Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork

A broad range of membrane proteins display anomalous diffusion on the cell surface. Different methods provide evidence for obstructed subdiffusion and diffusion on a fractal space, but the underlying structure inducing anomalous diffusion has never been visualized because of experimental challenges....

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Detalles Bibliográficos
Autores principales: Sadegh, Sanaz, Higgins, Jenny L., Mannion, Patrick C., Tamkun, Michael M., Krapf, Diego
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5500227/
https://www.ncbi.nlm.nih.gov/pubmed/28690919
http://dx.doi.org/10.1103/PhysRevX.7.011031
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author Sadegh, Sanaz
Higgins, Jenny L.
Mannion, Patrick C.
Tamkun, Michael M.
Krapf, Diego
author_facet Sadegh, Sanaz
Higgins, Jenny L.
Mannion, Patrick C.
Tamkun, Michael M.
Krapf, Diego
author_sort Sadegh, Sanaz
collection PubMed
description A broad range of membrane proteins display anomalous diffusion on the cell surface. Different methods provide evidence for obstructed subdiffusion and diffusion on a fractal space, but the underlying structure inducing anomalous diffusion has never been visualized because of experimental challenges. We addressed this problem by imaging the cortical actin at high resolution while simultaneously tracking individual membrane proteins in live mammalian cells. Our data confirm that actin introduces barriers leading to compartmentalization of the plasma membrane and that membrane proteins are transiently confined within actin fences. Furthermore, superresolution imaging shows that the cortical actin is organized into a self-similar meshwork. These results present a hierarchical nanoscale picture of the plasma membrane.
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spelling pubmed-55002272017-07-06 Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork Sadegh, Sanaz Higgins, Jenny L. Mannion, Patrick C. Tamkun, Michael M. Krapf, Diego Phys Rev X Article A broad range of membrane proteins display anomalous diffusion on the cell surface. Different methods provide evidence for obstructed subdiffusion and diffusion on a fractal space, but the underlying structure inducing anomalous diffusion has never been visualized because of experimental challenges. We addressed this problem by imaging the cortical actin at high resolution while simultaneously tracking individual membrane proteins in live mammalian cells. Our data confirm that actin introduces barriers leading to compartmentalization of the plasma membrane and that membrane proteins are transiently confined within actin fences. Furthermore, superresolution imaging shows that the cortical actin is organized into a self-similar meshwork. These results present a hierarchical nanoscale picture of the plasma membrane. 2017-03-09 2017 /pmc/articles/PMC5500227/ /pubmed/28690919 http://dx.doi.org/10.1103/PhysRevX.7.011031 Text en Published by the American Physical Society under the terms of the Creative Commons Attribution 4.0 International (https://creativecommons.org/licenses/by/4.0/) license. Further distribution of this work must maintain attribution to the author(s) and the published article’s title, journal citation, and DOI.
spellingShingle Article
Sadegh, Sanaz
Higgins, Jenny L.
Mannion, Patrick C.
Tamkun, Michael M.
Krapf, Diego
Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork
title Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork
title_full Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork
title_fullStr Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork
title_full_unstemmed Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork
title_short Plasma Membrane is Compartmentalized by a Self-Similar Cortical Actin Meshwork
title_sort plasma membrane is compartmentalized by a self-similar cortical actin meshwork
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5500227/
https://www.ncbi.nlm.nih.gov/pubmed/28690919
http://dx.doi.org/10.1103/PhysRevX.7.011031
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