Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle

Autores
Zhang, Tan; Taylor, Jackson; Jiang, Yang; Pereyra, Andrea Soledad; Messi, Maria Laura; Wang, Zhong Min; Hereñú, Claudia Beatriz; Delbono, Osvaldo
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The voltage-gated calcium channel (Cav) β1a subunit (Cavβ1a) plays an important role in excitation-contraction coupling (ECC), a process in the myoplasm that leads to muscle-force generation. Recently, we discovered that the Cavβ1a subunit travels to the nucleus of skeletal muscle cells where it helps to regulate gene transcription. To determine how it travels to the nucleus, we performed a yeast two-hybrid screening of the mouse fast skeletal muscle cDNA library and identified an interaction with troponin T3 (TnT3), which we subsequently confirmed by co-immunoprecipitation and co-localization assays in mouse skeletal muscle in vivo and in cultured C2C12 muscle cells. Interacting domains were mapped to the leucine zipper domain in TnT3 COOH-terminus (160-244 aa) and Cavβ1a NH2-terminus (1-99 aa), respectively. The double fluorescence assay in C2C12 cells co-expressing TnT3/DsRed and Cavβ1a/YFP shows that TnT3 facilitates Cavβ1a nuclear recruitment, suggesting that the two proteins play a heretofore unknown role during early muscle differentiation in addition to their classical role in ECC regulation.
Facultad de Ciencias Médicas
Materia
Ciencias Médicas
Biología
Cavβ1a
Nuclear localization
Skeletal muscle
Troponin T3
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/102639

id SEDICI_547a105f1f7e0fb3e7f7914995ec1f27
oai_identifier_str oai:sedici.unlp.edu.ar:10915/102639
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscleZhang, TanTaylor, JacksonJiang, YangPereyra, Andrea SoledadMessi, Maria LauraWang, Zhong MinHereñú, Claudia BeatrizDelbono, OsvaldoCiencias MédicasBiologíaCavβ1aNuclear localizationSkeletal muscleTroponin T3The voltage-gated calcium channel (Cav) β1a subunit (Cavβ1a) plays an important role in excitation-contraction coupling (ECC), a process in the myoplasm that leads to muscle-force generation. Recently, we discovered that the Cavβ1a subunit travels to the nucleus of skeletal muscle cells where it helps to regulate gene transcription. To determine how it travels to the nucleus, we performed a yeast two-hybrid screening of the mouse fast skeletal muscle cDNA library and identified an interaction with troponin T3 (TnT3), which we subsequently confirmed by co-immunoprecipitation and co-localization assays in mouse skeletal muscle in vivo and in cultured C2C12 muscle cells. Interacting domains were mapped to the leucine zipper domain in TnT3 COOH-terminus (160-244 aa) and Cavβ1a NH2-terminus (1-99 aa), respectively. The double fluorescence assay in C2C12 cells co-expressing TnT3/DsRed and Cavβ1a/YFP shows that TnT3 facilitates Cavβ1a nuclear recruitment, suggesting that the two proteins play a heretofore unknown role during early muscle differentiation in addition to their classical role in ECC regulation.Facultad de Ciencias Médicas2015-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf276-286http://sedici.unlp.edu.ar/handle/10915/102639enginfo:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/48902info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4522384/info:eu-repo/semantics/altIdentifier/issn/0014-4827info:eu-repo/semantics/altIdentifier/doi/10.1016/j.yexcr.2015.05.005info:eu-repo/semantics/altIdentifier/hdl/11336/48902info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-15T11:12:00Zoai:sedici.unlp.edu.ar:10915/102639Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-15 11:12:00.715SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
title Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
spellingShingle Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
Zhang, Tan
Ciencias Médicas
Biología
Cavβ1a
Nuclear localization
Skeletal muscle
Troponin T3
title_short Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
title_full Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
title_fullStr Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
title_full_unstemmed Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
title_sort Troponin T3 regulates nuclear localization of the calcium channel Cavβ1a subunit in skeletal muscle
dc.creator.none.fl_str_mv Zhang, Tan
Taylor, Jackson
Jiang, Yang
Pereyra, Andrea Soledad
Messi, Maria Laura
Wang, Zhong Min
Hereñú, Claudia Beatriz
Delbono, Osvaldo
author Zhang, Tan
author_facet Zhang, Tan
Taylor, Jackson
Jiang, Yang
Pereyra, Andrea Soledad
Messi, Maria Laura
Wang, Zhong Min
Hereñú, Claudia Beatriz
Delbono, Osvaldo
author_role author
author2 Taylor, Jackson
Jiang, Yang
Pereyra, Andrea Soledad
Messi, Maria Laura
Wang, Zhong Min
Hereñú, Claudia Beatriz
Delbono, Osvaldo
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Médicas
Biología
Cavβ1a
Nuclear localization
Skeletal muscle
Troponin T3
topic Ciencias Médicas
Biología
Cavβ1a
Nuclear localization
Skeletal muscle
Troponin T3
dc.description.none.fl_txt_mv The voltage-gated calcium channel (Cav) β1a subunit (Cavβ1a) plays an important role in excitation-contraction coupling (ECC), a process in the myoplasm that leads to muscle-force generation. Recently, we discovered that the Cavβ1a subunit travels to the nucleus of skeletal muscle cells where it helps to regulate gene transcription. To determine how it travels to the nucleus, we performed a yeast two-hybrid screening of the mouse fast skeletal muscle cDNA library and identified an interaction with troponin T3 (TnT3), which we subsequently confirmed by co-immunoprecipitation and co-localization assays in mouse skeletal muscle in vivo and in cultured C2C12 muscle cells. Interacting domains were mapped to the leucine zipper domain in TnT3 COOH-terminus (160-244 aa) and Cavβ1a NH2-terminus (1-99 aa), respectively. The double fluorescence assay in C2C12 cells co-expressing TnT3/DsRed and Cavβ1a/YFP shows that TnT3 facilitates Cavβ1a nuclear recruitment, suggesting that the two proteins play a heretofore unknown role during early muscle differentiation in addition to their classical role in ECC regulation.
Facultad de Ciencias Médicas
description The voltage-gated calcium channel (Cav) β1a subunit (Cavβ1a) plays an important role in excitation-contraction coupling (ECC), a process in the myoplasm that leads to muscle-force generation. Recently, we discovered that the Cavβ1a subunit travels to the nucleus of skeletal muscle cells where it helps to regulate gene transcription. To determine how it travels to the nucleus, we performed a yeast two-hybrid screening of the mouse fast skeletal muscle cDNA library and identified an interaction with troponin T3 (TnT3), which we subsequently confirmed by co-immunoprecipitation and co-localization assays in mouse skeletal muscle in vivo and in cultured C2C12 muscle cells. Interacting domains were mapped to the leucine zipper domain in TnT3 COOH-terminus (160-244 aa) and Cavβ1a NH2-terminus (1-99 aa), respectively. The double fluorescence assay in C2C12 cells co-expressing TnT3/DsRed and Cavβ1a/YFP shows that TnT3 facilitates Cavβ1a nuclear recruitment, suggesting that the two proteins play a heretofore unknown role during early muscle differentiation in addition to their classical role in ECC regulation.
publishDate 2015
dc.date.none.fl_str_mv 2015-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/102639
url http://sedici.unlp.edu.ar/handle/10915/102639
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://ri.conicet.gov.ar/11336/48902
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4522384/
info:eu-repo/semantics/altIdentifier/issn/0014-4827
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.yexcr.2015.05.005
info:eu-repo/semantics/altIdentifier/hdl/11336/48902
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
276-286
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
_version_ 1846064177453465600
score 13.22299