Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants

Abstract Four-domain voltage-gated cation channels (FVCCs) represent a large family of pseudo-tetrameric ion channels which includes voltage-gated calcium (Cav) and sodium (Nav) channels, as well as their homologues. These transmembrane proteins are involved in a wide range of physiological processe...

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Autores principales:	Ilya Pozdnyakov, Olga Matantseva, Sergei Skarlato
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f0cdf4d4922a4215bee102b359e75dd9
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spelling	oai:doaj.org-article:f0cdf4d4922a4215bee102b359e75dd92021-12-02T11:40:55ZDiversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants10.1038/s41598-018-21897-72045-2322https://doaj.org/article/f0cdf4d4922a4215bee102b359e75dd92018-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-018-21897-7https://doaj.org/toc/2045-2322Abstract Four-domain voltage-gated cation channels (FVCCs) represent a large family of pseudo-tetrameric ion channels which includes voltage-gated calcium (Cav) and sodium (Nav) channels, as well as their homologues. These transmembrane proteins are involved in a wide range of physiological processes, such as membrane excitability, rhythmical activity, intracellular signalling, etc. Information about actual diversity and phylogenetic relationships of FVCCs across the eukaryotic tree of life is scarce. We for the first time performed a taxonomically broad phylogenetic analysis of 277 FVCC sequences from a variety of eukaryotes and showed that many groups of eukaryotic organisms have their own clades of FVCCs. Moreover, the number of FVCC lineages in several groups of unicellular eukaryotes is comparable to that in animals. Based on the primary structure of FVCC sequences, we characterised their functional determinants (selectivity filter, voltage sensor, Nav-like inactivation gates, Cavβ-interaction motif, and calmodulin-binding region) and mapped them on the obtained phylogeny. This allowed uncovering of lineage-specific structural gains and losses in the course of FVCC evolution and identification of ancient structural features of these channels. Our results indicate that the ancestral FVCC was voltage-sensitive, possessed a Cav-like selectivity filter, Nav-like inactivation gates, calmodulin-binding motifs and did not bear the structure for Cavβ-binding.Ilya PozdnyakovOlga MatantsevaSergei SkarlatoNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 8, Iss 1, Pp 1-10 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ilya Pozdnyakov Olga Matantseva Sergei Skarlato Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants
description	Abstract Four-domain voltage-gated cation channels (FVCCs) represent a large family of pseudo-tetrameric ion channels which includes voltage-gated calcium (Cav) and sodium (Nav) channels, as well as their homologues. These transmembrane proteins are involved in a wide range of physiological processes, such as membrane excitability, rhythmical activity, intracellular signalling, etc. Information about actual diversity and phylogenetic relationships of FVCCs across the eukaryotic tree of life is scarce. We for the first time performed a taxonomically broad phylogenetic analysis of 277 FVCC sequences from a variety of eukaryotes and showed that many groups of eukaryotic organisms have their own clades of FVCCs. Moreover, the number of FVCC lineages in several groups of unicellular eukaryotes is comparable to that in animals. Based on the primary structure of FVCC sequences, we characterised their functional determinants (selectivity filter, voltage sensor, Nav-like inactivation gates, Cavβ-interaction motif, and calmodulin-binding region) and mapped them on the obtained phylogeny. This allowed uncovering of lineage-specific structural gains and losses in the course of FVCC evolution and identification of ancient structural features of these channels. Our results indicate that the ancestral FVCC was voltage-sensitive, possessed a Cav-like selectivity filter, Nav-like inactivation gates, calmodulin-binding motifs and did not bear the structure for Cavβ-binding.
format	article
author	Ilya Pozdnyakov Olga Matantseva Sergei Skarlato
author_facet	Ilya Pozdnyakov Olga Matantseva Sergei Skarlato
author_sort	Ilya Pozdnyakov
title	Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants
title_short	Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants
title_full	Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants
title_fullStr	Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants
title_full_unstemmed	Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants
title_sort	diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/f0cdf4d4922a4215bee102b359e75dd9
work_keys_str_mv	AT ilyapozdnyakov diversityandevolutionoffourdomainvoltagegatedcationchannelsofeukaryotesandtheirancestralfunctionaldeterminants AT olgamatantseva diversityandevolutionoffourdomainvoltagegatedcationchannelsofeukaryotesandtheirancestralfunctionaldeterminants AT sergeiskarlato diversityandevolutionoffourdomainvoltagegatedcationchannelsofeukaryotesandtheirancestralfunctionaldeterminants
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Diversity and evolution of four-domain voltage-gated cation channels of eukaryotes and their ancestral functional determinants

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