Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.

Interplay between cellular membranes and their peripheral proteins drives many processes in eukaryotic cells. Proteins of the Bin/Amphiphysin/Rvs (BAR) domain family, in particular, play a role in cellular morphogenesis, for example curving planar membranes into tubular membranes. However, it is sti...

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Auteurs principaux:	Hang Yu, Klaus Schulten
Format:	article
Langue:	EN
Publié:	Public Library of Science (PLoS) 2013
Sujets:	Biology (General) QH301-705.5
Accès en ligne:	https://doaj.org/article/e6ac1d5c2b5c4da58203acdae7acff34
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spelling	oai:doaj.org-article:e6ac1d5c2b5c4da58203acdae7acff342021-11-18T05:52:28ZMembrane sculpting by F-BAR domains studied by molecular dynamics simulations.1553-734X1553-735810.1371/journal.pcbi.1002892https://doaj.org/article/e6ac1d5c2b5c4da58203acdae7acff342013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23382665/pdf/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358Interplay between cellular membranes and their peripheral proteins drives many processes in eukaryotic cells. Proteins of the Bin/Amphiphysin/Rvs (BAR) domain family, in particular, play a role in cellular morphogenesis, for example curving planar membranes into tubular membranes. However, it is still unclear how F-BAR domain proteins act on membranes. Electron microscopy revealed that, in vitro, F-BAR proteins form regular lattices on cylindrically deformed membrane surfaces. Using all-atom and coarse-grained (CG) molecular dynamics simulations, we show that such lattices, indeed, induce tubes of observed radii. A 250 ns all-atom simulation reveals that F-BAR domain curves membranes via the so-called scaffolding mechanism. Plasticity of the F-BAR domain permits conformational change in response to membrane interaction, via partial unwinding of the domains 3-helix bundle structure. A CG simulation covering more than 350 µs provides a dynamic picture of membrane tubulation by lattices of F-BAR domains. A series of CG simulations identified the optimal lattice type for membrane sculpting, which matches closely the lattices seen through cryo-electron microscopy.Hang YuKlaus SchultenPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 9, Iss 1, p e1002892 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Hang Yu Klaus Schulten Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.
description	Interplay between cellular membranes and their peripheral proteins drives many processes in eukaryotic cells. Proteins of the Bin/Amphiphysin/Rvs (BAR) domain family, in particular, play a role in cellular morphogenesis, for example curving planar membranes into tubular membranes. However, it is still unclear how F-BAR domain proteins act on membranes. Electron microscopy revealed that, in vitro, F-BAR proteins form regular lattices on cylindrically deformed membrane surfaces. Using all-atom and coarse-grained (CG) molecular dynamics simulations, we show that such lattices, indeed, induce tubes of observed radii. A 250 ns all-atom simulation reveals that F-BAR domain curves membranes via the so-called scaffolding mechanism. Plasticity of the F-BAR domain permits conformational change in response to membrane interaction, via partial unwinding of the domains 3-helix bundle structure. A CG simulation covering more than 350 µs provides a dynamic picture of membrane tubulation by lattices of F-BAR domains. A series of CG simulations identified the optimal lattice type for membrane sculpting, which matches closely the lattices seen through cryo-electron microscopy.
format	article
author	Hang Yu Klaus Schulten
author_facet	Hang Yu Klaus Schulten
author_sort	Hang Yu
title	Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.
title_short	Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.
title_full	Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.
title_fullStr	Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.
title_full_unstemmed	Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.
title_sort	membrane sculpting by f-bar domains studied by molecular dynamics simulations.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/e6ac1d5c2b5c4da58203acdae7acff34
work_keys_str_mv	AT hangyu membranesculptingbyfbardomainsstudiedbymoleculardynamicssimulations AT klausschulten membranesculptingbyfbardomainsstudiedbymoleculardynamicssimulations
_version_	1718424762021052416

Membrane sculpting by F-BAR domains studied by molecular dynamics simulations.

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