Do calmodulin binding IQ motifs have built-in capping domains?

Most calmodulin (CaM) targets are α-helices. It is not clear if CaM induces the adoption of an α-helix configuration to its targets or if those targets are selected as they spontaneously adopt an α-helical conformation. Other than an α-helix propensity, there is a great variety of CaM targets with l...

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Autores: Muguruza-Montero, Arantza, Ramis, Rafael, Núñez, Eider, Ballesteros, Oscar R., Ibarluzea, Markel G., Araujo, Ariane, Alicante Martínez, Sara, Urrutia, Janire, Leonardo, Aritz, Bergara, Aitor, Villarroel, Álvaro
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/258412
Acceso en línea:http://hdl.handle.net/10261/258412
Access Level:acceso abierto
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spelling Do calmodulin binding IQ motifs have built-in capping domains?Muguruza-Montero, ArantzaRamis, RafaelNúñez, EiderBallesteros, Oscar R.Ibarluzea, Markel G.Araujo, ArianeAlicante Martínez, SaraUrrutia, JanireLeonardo, AritzBergara, AitorVillarroel, ÁlvaroMost calmodulin (CaM) targets are α-helices. It is not clear if CaM induces the adoption of an α-helix configuration to its targets or if those targets are selected as they spontaneously adopt an α-helical conformation. Other than an α-helix propensity, there is a great variety of CaM targets with little more in common. One exception to this rule is the IQ site that can be recognized in a number of targets, such as those ion channels belonging to the KCNQ family. Although there is negligible sequence similarity between the IQ motif and the docking site on SK2 channels, both adopt a similar three-dimensional disposition. The isolated SK2 target presents a pre-folded core region that becomes fully α-helical upon binding to CaM. The existence of this pre-folded state suggests the occurrence of capping within CaM targets. In this review, we examine the capping properties within the residues flanking this core domain, and relate known IQ motifs and capping.The Government of the Autonomous Community of the Basque Country (IT1165-19 and KK-2020/00110) and the Spanish Ministry of Science and Innovation (RTI2018-097839-B-100 to A.V. and PID2019-105488GB-I00 to A.B., A.L., and O.R.B.) and FEDER funds provided financial support for this work. A.M-M. is supported by predoctoral contracts from the Basque Government administered by University of the Basque Country.Peer reviewedWiley-VCHEusko JaurlaritzaAgencia Estatal de Investigación (España)Ministerio de Ciencia, Innovación y Universidades (España)European CommissionUniversidad del País VascoConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202220222021info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/258412reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-105488GB-I00info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-097839-B-100https://doi.org/10.1002/pro.4170Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2584122026-05-22T06:33:51Z
dc.title.none.fl_str_mv Do calmodulin binding IQ motifs have built-in capping domains?
title Do calmodulin binding IQ motifs have built-in capping domains?
spellingShingle Do calmodulin binding IQ motifs have built-in capping domains?
Muguruza-Montero, Arantza
title_short Do calmodulin binding IQ motifs have built-in capping domains?
title_full Do calmodulin binding IQ motifs have built-in capping domains?
title_fullStr Do calmodulin binding IQ motifs have built-in capping domains?
title_full_unstemmed Do calmodulin binding IQ motifs have built-in capping domains?
title_sort Do calmodulin binding IQ motifs have built-in capping domains?
dc.creator.none.fl_str_mv Muguruza-Montero, Arantza
Ramis, Rafael
Núñez, Eider
Ballesteros, Oscar R.
Ibarluzea, Markel G.
Araujo, Ariane
Alicante Martínez, Sara
Urrutia, Janire
Leonardo, Aritz
Bergara, Aitor
Villarroel, Álvaro
author Muguruza-Montero, Arantza
author_facet Muguruza-Montero, Arantza
Ramis, Rafael
Núñez, Eider
Ballesteros, Oscar R.
Ibarluzea, Markel G.
Araujo, Ariane
Alicante Martínez, Sara
Urrutia, Janire
Leonardo, Aritz
Bergara, Aitor
Villarroel, Álvaro
author_role author
author2 Ramis, Rafael
Núñez, Eider
Ballesteros, Oscar R.
Ibarluzea, Markel G.
Araujo, Ariane
Alicante Martínez, Sara
Urrutia, Janire
Leonardo, Aritz
Bergara, Aitor
Villarroel, Álvaro
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Eusko Jaurlaritza
Agencia Estatal de Investigación (España)
Ministerio de Ciencia, Innovación y Universidades (España)
European Commission
Universidad del País Vasco
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
description Most calmodulin (CaM) targets are α-helices. It is not clear if CaM induces the adoption of an α-helix configuration to its targets or if those targets are selected as they spontaneously adopt an α-helical conformation. Other than an α-helix propensity, there is a great variety of CaM targets with little more in common. One exception to this rule is the IQ site that can be recognized in a number of targets, such as those ion channels belonging to the KCNQ family. Although there is negligible sequence similarity between the IQ motif and the docking site on SK2 channels, both adopt a similar three-dimensional disposition. The isolated SK2 target presents a pre-folded core region that becomes fully α-helical upon binding to CaM. The existence of this pre-folded state suggests the occurrence of capping within CaM targets. In this review, we examine the capping properties within the residues flanking this core domain, and relate known IQ motifs and capping.
publishDate 2021
dc.date.none.fl_str_mv 2021
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/10261/258412
url http://hdl.handle.net/10261/258412
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-105488GB-I00
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-097839-B-100
https://doi.org/10.1002/pro.4170
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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