Molecular modeling of mechanosensory ion channel structural and functional features.

The DEG/ENaC (Degenerin/Epithelial Sodium Channel) protein family comprises related ion channel subunits from all metazoans, including humans. Members of this protein family play roles in several important biological processes such as transduction of mechanical stimuli, sodium re-absorption and bloo...

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Autores principales:	Renate Gessmann, Nikos Kourtis, Kyriacos Petratos, Nektarios Tavernarakis
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a50af0841b174a1d8d4a44366878577f
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spelling	oai:doaj.org-article:a50af0841b174a1d8d4a44366878577f2021-11-18T06:35:06ZMolecular modeling of mechanosensory ion channel structural and functional features.1932-620310.1371/journal.pone.0012814https://doaj.org/article/a50af0841b174a1d8d4a44366878577f2010-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20877470/?tool=EBIhttps://doaj.org/toc/1932-6203The DEG/ENaC (Degenerin/Epithelial Sodium Channel) protein family comprises related ion channel subunits from all metazoans, including humans. Members of this protein family play roles in several important biological processes such as transduction of mechanical stimuli, sodium re-absorption and blood pressure regulation. Several blocks of amino acid sequence are conserved in DEG/ENaC proteins, but structure/function relations in this channel class are poorly understood. Given the considerable experimental limitations associated with the crystallization of integral membrane proteins, knowledge-based modeling is often the only route towards obtaining reliable structural information. To gain insight into the structural characteristics of DEG/ENaC ion channels, we derived three-dimensional models of MEC-4 and UNC-8, based on the available crystal structures of ASIC1 (Acid Sensing Ion Channel 1). MEC-4 and UNC-8 are two DEG/ENaC family members involved in mechanosensation and proprioception respectively, in the nematode Caenorhabditis elegans. We used these models to examine the structural effects of specific mutations that alter channel function in vivo. The trimeric MEC-4 model provides insight into the mechanism by which gain-of-function mutations cause structural alterations that result in increased channel permeability, which trigger cell degeneration. Our analysis provides an introductory framework to further investigate the multimeric organization of the DEG/ENaC ion channel complex.Renate GessmannNikos KourtisKyriacos PetratosNektarios TavernarakisPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 9, p e12814 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Renate Gessmann Nikos Kourtis Kyriacos Petratos Nektarios Tavernarakis Molecular modeling of mechanosensory ion channel structural and functional features.
description	The DEG/ENaC (Degenerin/Epithelial Sodium Channel) protein family comprises related ion channel subunits from all metazoans, including humans. Members of this protein family play roles in several important biological processes such as transduction of mechanical stimuli, sodium re-absorption and blood pressure regulation. Several blocks of amino acid sequence are conserved in DEG/ENaC proteins, but structure/function relations in this channel class are poorly understood. Given the considerable experimental limitations associated with the crystallization of integral membrane proteins, knowledge-based modeling is often the only route towards obtaining reliable structural information. To gain insight into the structural characteristics of DEG/ENaC ion channels, we derived three-dimensional models of MEC-4 and UNC-8, based on the available crystal structures of ASIC1 (Acid Sensing Ion Channel 1). MEC-4 and UNC-8 are two DEG/ENaC family members involved in mechanosensation and proprioception respectively, in the nematode Caenorhabditis elegans. We used these models to examine the structural effects of specific mutations that alter channel function in vivo. The trimeric MEC-4 model provides insight into the mechanism by which gain-of-function mutations cause structural alterations that result in increased channel permeability, which trigger cell degeneration. Our analysis provides an introductory framework to further investigate the multimeric organization of the DEG/ENaC ion channel complex.
format	article
author	Renate Gessmann Nikos Kourtis Kyriacos Petratos Nektarios Tavernarakis
author_facet	Renate Gessmann Nikos Kourtis Kyriacos Petratos Nektarios Tavernarakis
author_sort	Renate Gessmann
title	Molecular modeling of mechanosensory ion channel structural and functional features.
title_short	Molecular modeling of mechanosensory ion channel structural and functional features.
title_full	Molecular modeling of mechanosensory ion channel structural and functional features.
title_fullStr	Molecular modeling of mechanosensory ion channel structural and functional features.
title_full_unstemmed	Molecular modeling of mechanosensory ion channel structural and functional features.
title_sort	molecular modeling of mechanosensory ion channel structural and functional features.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/a50af0841b174a1d8d4a44366878577f
work_keys_str_mv	AT renategessmann molecularmodelingofmechanosensoryionchannelstructuralandfunctionalfeatures AT nikoskourtis molecularmodelingofmechanosensoryionchannelstructuralandfunctionalfeatures AT kyriacospetratos molecularmodelingofmechanosensoryionchannelstructuralandfunctionalfeatures AT nektariostavernarakis molecularmodelingofmechanosensoryionchannelstructuralandfunctionalfeatures
_version_	1718424497944526848

Molecular modeling of mechanosensory ion channel structural and functional features.

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