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Long-Range Organization of Membrane-Curving Proteins

[Image: see text] Biological membranes have a central role in mediating the organization of membrane-curving proteins, a dynamic process that has proven to be challenging to probe experimentally. Using atomic force microscopy, we capture the hierarchically organized assemblies of Bin/amphiphysin/Rvs...

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Autores principales: Simunovic, Mijo, Šarić, Anđela, Henderson, J. Michael, Lee, Ka Yee C., Voth, Gregory A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2017
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5746856/
https://www.ncbi.nlm.nih.gov/pubmed/29296664
http://dx.doi.org/10.1021/acscentsci.7b00392
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author Simunovic, Mijo
Šarić, Anđela
Henderson, J. Michael
Lee, Ka Yee C.
Voth, Gregory A.
author_facet Simunovic, Mijo
Šarić, Anđela
Henderson, J. Michael
Lee, Ka Yee C.
Voth, Gregory A.
author_sort Simunovic, Mijo
collection PubMed
description [Image: see text] Biological membranes have a central role in mediating the organization of membrane-curving proteins, a dynamic process that has proven to be challenging to probe experimentally. Using atomic force microscopy, we capture the hierarchically organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid membranes. Their structure reveals distinct long linear aggregates of proteins, regularly spaced by up to 300 nm. Employing accurate free-energy calculations from large-scale coarse-grained computer simulations, we found that the membrane mediates the interaction among protein filaments as a combination of short- and long-ranged interactions. The long-ranged component acts at strikingly long distances, giving rise to a variety of micron-sized ordered patterns. This mechanism may contribute to the long-ranged spatiotemporal control of membrane remodeling by proteins in the cell.
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spelling pubmed-57468562018-01-02 Long-Range Organization of Membrane-Curving Proteins Simunovic, Mijo Šarić, Anđela Henderson, J. Michael Lee, Ka Yee C. Voth, Gregory A. ACS Cent Sci [Image: see text] Biological membranes have a central role in mediating the organization of membrane-curving proteins, a dynamic process that has proven to be challenging to probe experimentally. Using atomic force microscopy, we capture the hierarchically organized assemblies of Bin/amphiphysin/Rvs (BAR) proteins on supported lipid membranes. Their structure reveals distinct long linear aggregates of proteins, regularly spaced by up to 300 nm. Employing accurate free-energy calculations from large-scale coarse-grained computer simulations, we found that the membrane mediates the interaction among protein filaments as a combination of short- and long-ranged interactions. The long-ranged component acts at strikingly long distances, giving rise to a variety of micron-sized ordered patterns. This mechanism may contribute to the long-ranged spatiotemporal control of membrane remodeling by proteins in the cell. American Chemical Society 2017-11-21 2017-12-27 /pmc/articles/PMC5746856/ /pubmed/29296664 http://dx.doi.org/10.1021/acscentsci.7b00392 Text en Copyright © 2017 American Chemical Society This is an open access article published under a Creative Commons Attribution (CC-BY) License (http://pubs.acs.org/page/policy/authorchoice_ccby_termsofuse.html) , which permits unrestricted use, distribution and reproduction in any medium, provided the author and source are cited.
spellingShingle Simunovic, Mijo
Šarić, Anđela
Henderson, J. Michael
Lee, Ka Yee C.
Voth, Gregory A.
Long-Range Organization of Membrane-Curving Proteins
title Long-Range Organization of Membrane-Curving Proteins
title_full Long-Range Organization of Membrane-Curving Proteins
title_fullStr Long-Range Organization of Membrane-Curving Proteins
title_full_unstemmed Long-Range Organization of Membrane-Curving Proteins
title_short Long-Range Organization of Membrane-Curving Proteins
title_sort long-range organization of membrane-curving proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5746856/
https://www.ncbi.nlm.nih.gov/pubmed/29296664
http://dx.doi.org/10.1021/acscentsci.7b00392
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