Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands

The cation nonselective channel TRPM8 is activated by multiple stimuli, including moderate cold and various chemical compounds (i.e., menthol and icilin [Fig. 1], among others). While research continues growing on the under- standing of the physiological involvement of TRPM8 channels and their role...

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Detalles Bibliográficos
Autores: Plaza‐Cayón, Alejandro, González-Muñiz, Rosario, Martín-Martínez, Mercedes
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/279770
Acceso en línea:http://hdl.handle.net/10261/279770
Access Level:acceso abierto
Palabra clave:Agonist
Antagonists
Mutants
Structure
TRPM8
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spelling Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligandsPlaza‐Cayón, AlejandroGonzález-Muñiz, RosarioMartín-Martínez, MercedesAgonistAntagonistsMutantsStructureTRPM8The cation nonselective channel TRPM8 is activated by multiple stimuli, including moderate cold and various chemical compounds (i.e., menthol and icilin [Fig. 1], among others). While research continues growing on the under- standing of the physiological involvement of TRPM8 channels and their role in various pathological states, the information available on its activation mechanisms has also increased, supported by mutagenesis and structural stud- ies. This review compiles known information on specific mutations of channel residues and their consequences on channel viability and function. Besides, the comparison of sequence of animals living in different environments, together with chimera and mutagenesis studies are helping to unravel the mechanism of adaptation to different temperatures. The results of mutagenesis studies, grouped by different channel regions, are compared with the current knowledge of TRPM8 structures obtained by cryo‐electron microscopy. Trying to make this review self‐explicative and highly informative, important residues for TRPM8 function are summarized in a figure, and mutants, deletions and chimeras are compiled in a table, including also the observed effects by different methods of activation and the corresponding references. The information provided by this review may also help in the design of new ligands for TRPM8, an interesting biological target for therapeutic interventionThis study was funded by grants from the Spanish Ministerio de Ciencia, Innovación y Universidades, Agencia Estatal de Investigación and Fondo Europeo de Desarrollo Regional (MICIU/AEI/FEDER, UE), grant number RTI2018‐097189‐B‐C22 to R. G. M. and M. M. M., and CSIC grant numbers 201880E109 and 2019E030 to M. M. M. and R. G. M., respectively. A. P. C. thanks CSIC and IQM for a JAE Intro ICUs granPeer reviewedWiley-VCHMinisterio de Ciencia, Innovación y Universidades (España)European CommissionConsejo Superior de Investigaciones Científicas (España)Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202220222022info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/279770reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1002/med.21920Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2797702026-05-22T06:33:51Z
dc.title.none.fl_str_mv Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
title Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
spellingShingle Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
Plaza‐Cayón, Alejandro
Agonist
Antagonists
Mutants
Structure
TRPM8
title_short Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
title_full Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
title_fullStr Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
title_full_unstemmed Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
title_sort Mutations of TRPM8 channels: Unraveling the molecular basis of activation by cold and ligands
dc.creator.none.fl_str_mv Plaza‐Cayón, Alejandro
González-Muñiz, Rosario
Martín-Martínez, Mercedes
author Plaza‐Cayón, Alejandro
author_facet Plaza‐Cayón, Alejandro
González-Muñiz, Rosario
Martín-Martínez, Mercedes
author_role author
author2 González-Muñiz, Rosario
Martín-Martínez, Mercedes
author2_role author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia, Innovación y Universidades (España)
European Commission
Consejo Superior de Investigaciones Científicas (España)
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Agonist
Antagonists
Mutants
Structure
TRPM8
topic Agonist
Antagonists
Mutants
Structure
TRPM8
description The cation nonselective channel TRPM8 is activated by multiple stimuli, including moderate cold and various chemical compounds (i.e., menthol and icilin [Fig. 1], among others). While research continues growing on the under- standing of the physiological involvement of TRPM8 channels and their role in various pathological states, the information available on its activation mechanisms has also increased, supported by mutagenesis and structural stud- ies. This review compiles known information on specific mutations of channel residues and their consequences on channel viability and function. Besides, the comparison of sequence of animals living in different environments, together with chimera and mutagenesis studies are helping to unravel the mechanism of adaptation to different temperatures. The results of mutagenesis studies, grouped by different channel regions, are compared with the current knowledge of TRPM8 structures obtained by cryo‐electron microscopy. Trying to make this review self‐explicative and highly informative, important residues for TRPM8 function are summarized in a figure, and mutants, deletions and chimeras are compiled in a table, including also the observed effects by different methods of activation and the corresponding references. The information provided by this review may also help in the design of new ligands for TRPM8, an interesting biological target for therapeutic intervention
publishDate 2022
dc.date.none.fl_str_mv 2022
2022
2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/279770
url http://hdl.handle.net/10261/279770
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1002/med.21920
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Wiley-VCH
publisher.none.fl_str_mv Wiley-VCH
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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