citation_keywords: lipid-protein interactions; annular lipids; lens aquaporin-0; molecular dynamics simulations; Hydrophobic matching; lipid thinning; membrane protein association; membrane protein lipid sorting
citation_publication_date: 2017/03/02
citation_title: Localization and Ordering of Lipids Around Aquaporin-0: Protein and Lipid Mobility Effects
citation_author_institution: Computational Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany
Description: Hydrophobic matching, lipid sorting, and protein oligomerization are key principles by which lipids and proteins organize in biological membranes.The Aquaporin-0 channel (AQP0), solved by electron crystallography (EC) at cryogenic temperatures,is one of the few protein-lipid complexes of which the structure is available in atomic detail.EC and room-temperature molecular dynamics (MD) of dimyristoylglycerophosphocholine (DMPC) annular lipids around AQP0show similarities, however, crystal-packing and temperature might affect the protein surface or the lipids distribution.To understand the role of temperature, lipid phase, and protein mobility in the localization and ordering of AQP0-lipids,we used MD simulations of an AQP0-DMPC bilayer system.Simulations were performed at physiological and at DMPC gel-phase temperatures.To decouple the protein and lipid mobility effects, we induced gel-phase in the lipidsor restrained the protein.We monitored the lipid ordering effects around the protein.Reducing the system temperature or inducing lipid gel-phase had a marginal effect on the annular lipid localization.However, restraining the protein mobility increased the annular lipid localization around the whole AQP0 surface, resembling EC.The distribution of the inter-phosphate and hydrophobic thicknessesshowed that stretching of the DMPC annular layer around AQP0 surface is the mechanism that compensates the hydrophobic mismatch in this system.The distribution of the local area-per-lip...
Keywords: lipid-protein interactions, annular lipids, lens aquaporin-0, molecular dynamics simulations, Hydrophobic matching, lipid thinning, membrane protein association, membrane protein lipid sorting
citation_publisher: Frontiers
citation_journal_title: Frontiers in Physiology
description: Hydrophobic matching, lipid sorting, and protein oligomerization are key principles by which lipids and proteins organize in biological membranes. The Aquaporin-0 channel (AQP0), solved by electron crystallography (EC) at cryogenic temperatures, is one of the few protein-lipid complexes of which the structure is available in atomic detail. EC and room-temperature molecular dynamics (MD) of dimyristoylglycerophosphocholine (DMPC) annular lipids around AQP0 show similarities, however, crystal-packing and temperature might affect the protein surface or the lipids distribution. To understand the role of temperature, lipid phase, and protein mobility in the localization and ordering of AQP0-lipids, we used MD simulations of an AQP0-DMPC bilayer system. Simulations were performed at physiological and at DMPC gel-phase temperatures. To decouple the protein and lipid mobility effects, we induced gel-phase in the lipids or restrained the protein. We monitored the lipid ordering effects around the protein. Reducing the system temperature or inducing lipid gel-phase had a marginal effect on the annular lipid localization. However, restraining the protein mobility increased the annular lipid localization around the whole AQP0 surface, resembling EC. The distribution of the inter-phosphate and hydrophobic thicknesses showed that stretching of the DMPC annular layer around AQP0 surface is the mechanism that compensates the hydrophobic mismatch in this system. The distribution of the local area-per-lipid and the acyl-chain order parameters showed particular fluid- and gel-like areas that involved several lipid layers. These areas were in contact with the surfaces of higher and lower protein mobility, respectively. We conclude that the AQP0 surfaces induce specific fluid- and gel-phase prone areas. The presence of these areas might guide {\color{red}the AQP0 lipid sorting} interactions with other membrane components, and is compatible with the {\color{red}squared array oligomerization} of AQP0 tetramers separated by a layer of annular lipids.
citation_date: 2017
title: Frontiers | Localization and Ordering of Lipids Around Aquaporin-0: Protein and Lipid Mobility Effects | Membrane Physiology and Membrane Biophysics
citation_author_email: 
citation_online_date: 2017/02/15
citation_issn: 1664-042X
dc:title: Frontiers | Localization and Ordering of Lipids Around Aquaporin-0: Protein and Lipid Mobility Effects | Membrane Physiology and Membrane Biophysics
citation_language: English
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citation_journal_abbrev: Front. Physiol.
citation_abstract: Hydrophobic matching, lipid sorting, and protein oligomerization are key principles by which lipids and proteins organize in biological membranes. The Aquaporin-0 channel (AQP0), solved by electron crystallography (EC) at cryogenic temperatures, is one of the few protein-lipid complexes of which the structure is available in atomic detail. EC and room-temperature molecular dynamics (MD) of dimyristoylglycerophosphocholine (DMPC) annular lipids around AQP0 show similarities, however, crystal-packing and temperature might affect the protein surface or the lipids distribution. To understand the role of temperature, lipid phase, and protein mobility in the localization and ordering of AQP0-lipids, we used MD simulations of an AQP0-DMPC bilayer system. Simulations were performed at physiological and at DMPC gel-phase temperatures. To decouple the protein and lipid mobility effects, we induced gel-phase in the lipids or restrained the protein. We monitored the lipid ordering effects around the protein. Reducing the system temperature or inducing lipid gel-phase had a marginal effect on the annular lipid localization. However, restraining the protein mobility increased the annular lipid localization around the whole AQP0 surface, resembling EC. The distribution of the inter-phosphate and hydrophobic thicknesses showed that stretching of the DMPC annular layer around AQP0 surface is the mechanism that compensates the hydrophobic mismatch in this system. The distribution of the local area-per-lipid and the acyl-chain order parameters showed particular fluid- and gel-like areas that involved several lipid layers. These areas were in contact with the surfaces of higher and lower protein mobility, respectively. We conclude that the AQP0 surfaces induce specific fluid- and gel-phase prone areas. The presence of these areas might guide {\color{red}the AQP0 lipid sorting} interactions with other membrane components, and is compatible with the {\color{red}squared array oligomerization} of AQP0 tetramers separated by a layer of annular lipids.
citation_author: Briones, Rodolfo
Title: Localization and Ordering of Lipids Around Aquaporin-0: Protein and Lipid Mobility Effects
citation_pages: 124
citation_abstract_html_url: http://journal.frontiersin.org/article/10.3389/fphys.2017.00124/abstract
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citation_doi: 10.3389/fphys.2017.00124
dc.identifier: doi:10.3389/fphys.2017.00124
citation_volume: 8
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