TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1

Transient receptor potential melastatin 7 (TRPM7) represents melastatin TRP channel with two significant functions, cation permeability and kinase activity. TRPM7 is widely expressed among tissues and is therefore involved in a variety of cellular functions representing mainly Mg2+ homeostasis, cell...

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Autores principales:	Kristyna Bousova, Monika Zouharova, Petr Herman, Veronika Vetyskova, Katerina Jiraskova, Jiri Vondrasek
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	TRPM7 Binding region CaM S100A1 Calcium Fluorescence anisotropy Science (General) Q1-390 Social sciences (General) H1-99
Acceso en línea:	https://doaj.org/article/245cb55ef8244ca0b6df6edb26d2422a
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spelling	oai:doaj.org-article:245cb55ef8244ca0b6df6edb26d2422a2021-12-02T05:03:26ZTRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A12405-844010.1016/j.heliyon.2021.e08490https://doaj.org/article/245cb55ef8244ca0b6df6edb26d2422a2021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2405844021025937https://doaj.org/toc/2405-8440Transient receptor potential melastatin 7 (TRPM7) represents melastatin TRP channel with two significant functions, cation permeability and kinase activity. TRPM7 is widely expressed among tissues and is therefore involved in a variety of cellular functions representing mainly Mg2+ homeostasis, cellular Ca2+ flickering, and the regulation of DNA transcription by a cleaved kinase domain translocated to the nucleus. TRPM7 participates in several important biological processes in the nervous and cardiovascular systems. Together with the necessary function of the TRPM7 in these tissues and its recently analyzed overall structure, this channel requires further studies leading to the development of potential therapeutic targets. Here we present the first study investigating the N-termini of TRPM7 with binding regions for important intracellular modulators calmodulin (CaM) and calcium-binding protein S1 (S100A1) using in vitro and in silico approaches. Molecular simulations of the discovered complexes reveal their potential binding interfaces with common interaction patterns and the important role of basic residues present in the N-terminal binding region of TRPM.Kristyna BousovaMonika ZouharovaPetr HermanVeronika VetyskovaKaterina JiraskovaJiri VondrasekElsevierarticleTRPM7Binding regionCaMS100A1CalciumFluorescence anisotropyScience (General)Q1-390Social sciences (General)H1-99ENHeliyon, Vol 7, Iss 12, Pp e08490- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	TRPM7 Binding region CaM S100A1 Calcium Fluorescence anisotropy Science (General) Q1-390 Social sciences (General) H1-99
spellingShingle	TRPM7 Binding region CaM S100A1 Calcium Fluorescence anisotropy Science (General) Q1-390 Social sciences (General) H1-99 Kristyna Bousova Monika Zouharova Petr Herman Veronika Vetyskova Katerina Jiraskova Jiri Vondrasek TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
description	Transient receptor potential melastatin 7 (TRPM7) represents melastatin TRP channel with two significant functions, cation permeability and kinase activity. TRPM7 is widely expressed among tissues and is therefore involved in a variety of cellular functions representing mainly Mg2+ homeostasis, cellular Ca2+ flickering, and the regulation of DNA transcription by a cleaved kinase domain translocated to the nucleus. TRPM7 participates in several important biological processes in the nervous and cardiovascular systems. Together with the necessary function of the TRPM7 in these tissues and its recently analyzed overall structure, this channel requires further studies leading to the development of potential therapeutic targets. Here we present the first study investigating the N-termini of TRPM7 with binding regions for important intracellular modulators calmodulin (CaM) and calcium-binding protein S1 (S100A1) using in vitro and in silico approaches. Molecular simulations of the discovered complexes reveal their potential binding interfaces with common interaction patterns and the important role of basic residues present in the N-terminal binding region of TRPM.
format	article
author	Kristyna Bousova Monika Zouharova Petr Herman Veronika Vetyskova Katerina Jiraskova Jiri Vondrasek
author_facet	Kristyna Bousova Monika Zouharova Petr Herman Veronika Vetyskova Katerina Jiraskova Jiri Vondrasek
author_sort	Kristyna Bousova
title	TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
title_short	TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
title_full	TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
title_fullStr	TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
title_full_unstemmed	TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1
title_sort	trpm7 n-terminal region forms complexes with calcium binding proteins cam and s100a1
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/245cb55ef8244ca0b6df6edb26d2422a
work_keys_str_mv	AT kristynabousova trpm7nterminalregionformscomplexeswithcalciumbindingproteinscamands100a1 AT monikazouharova trpm7nterminalregionformscomplexeswithcalciumbindingproteinscamands100a1 AT petrherman trpm7nterminalregionformscomplexeswithcalciumbindingproteinscamands100a1 AT veronikavetyskova trpm7nterminalregionformscomplexeswithcalciumbindingproteinscamands100a1 AT katerinajiraskova trpm7nterminalregionformscomplexeswithcalciumbindingproteinscamands100a1 AT jirivondrasek trpm7nterminalregionformscomplexeswithcalciumbindingproteinscamands100a1
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TRPM7 N-terminal region forms complexes with calcium binding proteins CaM and S100A1

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