Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility

Autores
Franchini, Lucia Florencia; Elgoyhen, Ana Belen
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Somatic electromotility in cochlear outer hair cells, as the basis for cochlear amplification, is a mammalian novelty and it is largely dependent upon rapid cell length changes proposed to be mediated by the motor-protein prestin, a member of the solute carrier anion-transport family 26. Thus, one might predict that prestin has specifically evolved in mammals to support this unique mammalian adaptation. Using codon-based likelihood models we found evidences for positive selection in the motor-protein prestin only in the mammalian lineage, supporting the hypothesis that lineage-specific adaptation-driven molecular changes endowed prestin with the ability to mediate somatic electromotility. Moreover, signatures of positive selection were found on the α10, but not the α9, nicotinic cholinergic receptor subunits. An α9α10-containing nicotinic cholinergic receptor mediates inhibitory olivocochlear efferent effects on hair cells across vertebrates. Our results suggest that evolution-driven modifications of the α10 subunit probably allowed the α9α10 heteromeric receptor to serve a differential function in the mammalian cochlea. Thus, we describe for the first time at the molecular level signatures of adaptive evolution in two outer hair cell proteins only in the lineage leading to mammals. This finding is most likely related with the roles these proteins play in somatic electromotility and/or its fine tuning.
Fil: Franchini, Lucia Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Elgoyhen, Ana Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires; Argentina
Materia
Acetylcholine
Adaptive Evolution
Hearing
Nicotinic Receptors
Outer Hair Cells
Prestin
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/79650
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/79650
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotilityFranchini, Lucia FlorenciaElgoyhen, Ana BelenAcetylcholineAdaptive EvolutionHearingNicotinic ReceptorsOuter Hair CellsPrestinhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Somatic electromotility in cochlear outer hair cells, as the basis for cochlear amplification, is a mammalian novelty and it is largely dependent upon rapid cell length changes proposed to be mediated by the motor-protein prestin, a member of the solute carrier anion-transport family 26. Thus, one might predict that prestin has specifically evolved in mammals to support this unique mammalian adaptation. Using codon-based likelihood models we found evidences for positive selection in the motor-protein prestin only in the mammalian lineage, supporting the hypothesis that lineage-specific adaptation-driven molecular changes endowed prestin with the ability to mediate somatic electromotility. Moreover, signatures of positive selection were found on the α10, but not the α9, nicotinic cholinergic receptor subunits. An α9α10-containing nicotinic cholinergic receptor mediates inhibitory olivocochlear efferent effects on hair cells across vertebrates. Our results suggest that evolution-driven modifications of the α10 subunit probably allowed the α9α10 heteromeric receptor to serve a differential function in the mammalian cochlea. Thus, we describe for the first time at the molecular level signatures of adaptive evolution in two outer hair cell proteins only in the lineage leading to mammals. This finding is most likely related with the roles these proteins play in somatic electromotility and/or its fine tuning.Fil: Franchini, Lucia Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; ArgentinaFil: Elgoyhen, Ana Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires; ArgentinaAcademic Press Inc Elsevier Science2006-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/79650Franchini, Lucia Florencia; Elgoyhen, Ana Belen; Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility; Academic Press Inc Elsevier Science; Molecular Phylogenetics and Evolution; 41; 3; 12-2006; 622-6351055-7903CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.ympev.2006.05.042info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1055790306002016info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:08:03Zoai:ri.conicet.gov.ar:11336/79650instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:08:03.471CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
title Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
spellingShingle Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
Franchini, Lucia Florencia
Acetylcholine
Adaptive Evolution
Hearing
Nicotinic Receptors
Outer Hair Cells
Prestin
title_short Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
title_full Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
title_fullStr Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
title_full_unstemmed Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
title_sort Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility
dc.creator.none.fl_str_mv Franchini, Lucia Florencia
Elgoyhen, Ana Belen
author Franchini, Lucia Florencia
author_facet Franchini, Lucia Florencia
Elgoyhen, Ana Belen
author_role author
author2 Elgoyhen, Ana Belen
author2_role author
dc.subject.none.fl_str_mv Acetylcholine
Adaptive Evolution
Hearing
Nicotinic Receptors
Outer Hair Cells
Prestin
topic Acetylcholine
Adaptive Evolution
Hearing
Nicotinic Receptors
Outer Hair Cells
Prestin
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Somatic electromotility in cochlear outer hair cells, as the basis for cochlear amplification, is a mammalian novelty and it is largely dependent upon rapid cell length changes proposed to be mediated by the motor-protein prestin, a member of the solute carrier anion-transport family 26. Thus, one might predict that prestin has specifically evolved in mammals to support this unique mammalian adaptation. Using codon-based likelihood models we found evidences for positive selection in the motor-protein prestin only in the mammalian lineage, supporting the hypothesis that lineage-specific adaptation-driven molecular changes endowed prestin with the ability to mediate somatic electromotility. Moreover, signatures of positive selection were found on the α10, but not the α9, nicotinic cholinergic receptor subunits. An α9α10-containing nicotinic cholinergic receptor mediates inhibitory olivocochlear efferent effects on hair cells across vertebrates. Our results suggest that evolution-driven modifications of the α10 subunit probably allowed the α9α10 heteromeric receptor to serve a differential function in the mammalian cochlea. Thus, we describe for the first time at the molecular level signatures of adaptive evolution in two outer hair cell proteins only in the lineage leading to mammals. This finding is most likely related with the roles these proteins play in somatic electromotility and/or its fine tuning.
Fil: Franchini, Lucia Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina
Fil: Elgoyhen, Ana Belen. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Investigaciones en Ingeniería Genética y Biología Molecular "Dr. Héctor N. Torres"; Argentina. Universidad de Buenos Aires; Argentina
description Somatic electromotility in cochlear outer hair cells, as the basis for cochlear amplification, is a mammalian novelty and it is largely dependent upon rapid cell length changes proposed to be mediated by the motor-protein prestin, a member of the solute carrier anion-transport family 26. Thus, one might predict that prestin has specifically evolved in mammals to support this unique mammalian adaptation. Using codon-based likelihood models we found evidences for positive selection in the motor-protein prestin only in the mammalian lineage, supporting the hypothesis that lineage-specific adaptation-driven molecular changes endowed prestin with the ability to mediate somatic electromotility. Moreover, signatures of positive selection were found on the α10, but not the α9, nicotinic cholinergic receptor subunits. An α9α10-containing nicotinic cholinergic receptor mediates inhibitory olivocochlear efferent effects on hair cells across vertebrates. Our results suggest that evolution-driven modifications of the α10 subunit probably allowed the α9α10 heteromeric receptor to serve a differential function in the mammalian cochlea. Thus, we describe for the first time at the molecular level signatures of adaptive evolution in two outer hair cell proteins only in the lineage leading to mammals. This finding is most likely related with the roles these proteins play in somatic electromotility and/or its fine tuning.
publishDate 2006
dc.date.none.fl_str_mv 2006-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/79650
Franchini, Lucia Florencia; Elgoyhen, Ana Belen; Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility; Academic Press Inc Elsevier Science; Molecular Phylogenetics and Evolution; 41; 3; 12-2006; 622-635
1055-7903
CONICET Digital
CONICET
url http://hdl.handle.net/11336/79650
identifier_str_mv Franchini, Lucia Florencia; Elgoyhen, Ana Belen; Adaptive evolution in mammalian proteins involved in cochlear outer hair cell electromotility; Academic Press Inc Elsevier Science; Molecular Phylogenetics and Evolution; 41; 3; 12-2006; 622-635
1055-7903
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ympev.2006.05.042
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1055790306002016
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.13397

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