The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics

The transient receptor potential melastatin-subfamily member 7 (TRPM7) is a ubiquitously expressed membrane protein consisting of ion channel and protein kinase domains. TRPM7 plays a fundamental role in the cellular uptake of divalent cations such as Zn2+, Mg2+, and Ca2+, and thus shapes cellular e...

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Autores principales:	Astrid Kollewe, Vladimir Chubanov, Fong Tsuen Tseung, Leonor Correia, Eva Schmidt, Anna Rössig, Susanna Zierler, Alexander Haupt, Catrin Swantje Müller, Wolfgang Bildl, Uwe Schulte, Annette Nicke, Bernd Fakler, Thomas Gudermann
Formato:	article
Lenguaje:	EN
Publicado:	eLife Sciences Publications Ltd 2021
Materias:	brain proteome TRPM7 complexes mouse human Xenopus Medicine R Science Q Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/069728908b0a4dfe9645de8e3e8aa566
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spelling	oai:doaj.org-article:069728908b0a4dfe9645de8e3e8aa5662021-11-25T10:45:33ZThe molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics10.7554/eLife.685442050-084Xe68544https://doaj.org/article/069728908b0a4dfe9645de8e3e8aa5662021-11-01T00:00:00Zhttps://elifesciences.org/articles/68544https://doaj.org/toc/2050-084XThe transient receptor potential melastatin-subfamily member 7 (TRPM7) is a ubiquitously expressed membrane protein consisting of ion channel and protein kinase domains. TRPM7 plays a fundamental role in the cellular uptake of divalent cations such as Zn2+, Mg2+, and Ca2+, and thus shapes cellular excitability, plasticity, and metabolic activity. The molecular appearance and operation of TRPM7 channels in native tissues have remained unresolved. Here, we investigated the subunit composition of endogenous TRPM7 channels in rodent brain by multi-epitope affinity purification and high-resolution quantitative mass spectrometry (MS) analysis. We found that native TRPM7 channels are high-molecular-weight multi-protein complexes that contain the putative metal transporter proteins CNNM1-4 and a small G-protein ADP-ribosylation factor-like protein 15 (ARL15). Heterologous reconstitution experiments confirmed the formation of TRPM7/CNNM/ARL15 ternary complexes and indicated that complex formation effectively and specifically impacts TRPM7 activity. These results open up new avenues towards a mechanistic understanding of the cellular regulation and function of TRPM7 channels.Astrid KolleweVladimir ChubanovFong Tsuen TseungLeonor CorreiaEva SchmidtAnna RössigSusanna ZierlerAlexander HauptCatrin Swantje MüllerWolfgang BildlUwe SchulteAnnette NickeBernd FaklerThomas GudermanneLife Sciences Publications LtdarticlebrainproteomeTRPM7 complexesmousehumanXenopusMedicineRScienceQBiology (General)QH301-705.5ENeLife, Vol 10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	brain proteome TRPM7 complexes mouse human Xenopus Medicine R Science Q Biology (General) QH301-705.5
spellingShingle	brain proteome TRPM7 complexes mouse human Xenopus Medicine R Science Q Biology (General) QH301-705.5 Astrid Kollewe Vladimir Chubanov Fong Tsuen Tseung Leonor Correia Eva Schmidt Anna Rössig Susanna Zierler Alexander Haupt Catrin Swantje Müller Wolfgang Bildl Uwe Schulte Annette Nicke Bernd Fakler Thomas Gudermann The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics
description	The transient receptor potential melastatin-subfamily member 7 (TRPM7) is a ubiquitously expressed membrane protein consisting of ion channel and protein kinase domains. TRPM7 plays a fundamental role in the cellular uptake of divalent cations such as Zn2+, Mg2+, and Ca2+, and thus shapes cellular excitability, plasticity, and metabolic activity. The molecular appearance and operation of TRPM7 channels in native tissues have remained unresolved. Here, we investigated the subunit composition of endogenous TRPM7 channels in rodent brain by multi-epitope affinity purification and high-resolution quantitative mass spectrometry (MS) analysis. We found that native TRPM7 channels are high-molecular-weight multi-protein complexes that contain the putative metal transporter proteins CNNM1-4 and a small G-protein ADP-ribosylation factor-like protein 15 (ARL15). Heterologous reconstitution experiments confirmed the formation of TRPM7/CNNM/ARL15 ternary complexes and indicated that complex formation effectively and specifically impacts TRPM7 activity. These results open up new avenues towards a mechanistic understanding of the cellular regulation and function of TRPM7 channels.
format	article
author	Astrid Kollewe Vladimir Chubanov Fong Tsuen Tseung Leonor Correia Eva Schmidt Anna Rössig Susanna Zierler Alexander Haupt Catrin Swantje Müller Wolfgang Bildl Uwe Schulte Annette Nicke Bernd Fakler Thomas Gudermann
author_facet	Astrid Kollewe Vladimir Chubanov Fong Tsuen Tseung Leonor Correia Eva Schmidt Anna Rössig Susanna Zierler Alexander Haupt Catrin Swantje Müller Wolfgang Bildl Uwe Schulte Annette Nicke Bernd Fakler Thomas Gudermann
author_sort	Astrid Kollewe
title	The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics
title_short	The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics
title_full	The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics
title_fullStr	The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics
title_full_unstemmed	The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics
title_sort	molecular appearance of native trpm7 channel complexes identified by high-resolution proteomics
publisher	eLife Sciences Publications Ltd
publishDate	2021
url	https://doaj.org/article/069728908b0a4dfe9645de8e3e8aa566
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The molecular appearance of native TRPM7 channel complexes identified by high-resolution proteomics

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