Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2
- Autores
- Zamponi, Emiliano; Buratti, Fiamma; Cataldi, Gabriel Enrique; Caicedo, Hector Hugo; Song, Yuyu; Jungbauer, Lisa M.; LaDu, Mary J.; Bisbal, Mariano; Lorenzo, Alfredo Guillermo; Ma, Jiyan; Helguera, Pablo Rodolfo; Morfini, Gerardo Andres; Brady, Scott T.; Pigino, Gustavo Fernando
- Año de publicación
- 2017
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Prion diseases include a number of progressive neuropathies involving conformational changes in cellular prion protein (PrPc) that may be fatal sporadic, familial or infectious. Pathological evidence indicated that neurons affected in prion diseases follow a dying-back pattern of degeneration. However, specific cellular processes affected by PrPc that explain such a pattern have not yet been identified. Results from cell biological and pharmacological experiments in isolated squid axoplasm and primary cultured neurons reveal inhibition of fast axonal transport (FAT) as a novel toxic effect elicited by PrPc. Pharmacological, biochemical and cell biological experiments further indicate this toxic effect involves casein kinase 2 (CK2) activation, providing a molecular basis for the toxic effect of PrPc on FAT. CK2 was found to phosphorylate and inhibit light chain subunits of the major motor protein conventional kinesin. Collectively, these findings suggest CK2 as a novel therapeutic target to prevent the gradual loss of neuronal connectivity that characterizes prion diseases.
Fil: Zamponi, Emiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Buratti, Fiamma. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Cataldi, Gabriel Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Caicedo, Hector Hugo. University of Illinois at Chicago; Estados Unidos
Fil: Song, Yuyu. Harvard Medical School; Estados Unidos
Fil: Jungbauer, Lisa M.. University of Illinois at Chicago; Estados Unidos
Fil: LaDu, Mary J.. University of Illinois at Chicago; Estados Unidos
Fil: Bisbal, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Lorenzo, Alfredo Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Ma, Jiyan. Van Andel Research Institute; Estados Unidos
Fil: Helguera, Pablo Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Morfini, Gerardo Andres. University of Illinois at Chicago; Estados Unidos
Fil: Brady, Scott T.. University of Illinois at Chicago; Estados Unidos
Fil: Pigino, Gustavo Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina. University of Illinois at Chicago; Estados Unidos - Materia
-
Fast axonal transport
Prion protein
Casein kinase 2 (CK2)
Neuropathies - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/64239
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Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2Zamponi, EmilianoBuratti, FiammaCataldi, Gabriel EnriqueCaicedo, Hector HugoSong, YuyuJungbauer, Lisa M.LaDu, Mary J.Bisbal, MarianoLorenzo, Alfredo GuillermoMa, JiyanHelguera, Pablo RodolfoMorfini, Gerardo AndresBrady, Scott T.Pigino, Gustavo FernandoFast axonal transportPrion proteinCasein kinase 2 (CK2)Neuropathieshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Prion diseases include a number of progressive neuropathies involving conformational changes in cellular prion protein (PrPc) that may be fatal sporadic, familial or infectious. Pathological evidence indicated that neurons affected in prion diseases follow a dying-back pattern of degeneration. However, specific cellular processes affected by PrPc that explain such a pattern have not yet been identified. Results from cell biological and pharmacological experiments in isolated squid axoplasm and primary cultured neurons reveal inhibition of fast axonal transport (FAT) as a novel toxic effect elicited by PrPc. Pharmacological, biochemical and cell biological experiments further indicate this toxic effect involves casein kinase 2 (CK2) activation, providing a molecular basis for the toxic effect of PrPc on FAT. CK2 was found to phosphorylate and inhibit light chain subunits of the major motor protein conventional kinesin. Collectively, these findings suggest CK2 as a novel therapeutic target to prevent the gradual loss of neuronal connectivity that characterizes prion diseases.Fil: Zamponi, Emiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Buratti, Fiamma. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Cataldi, Gabriel Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Caicedo, Hector Hugo. University of Illinois at Chicago; Estados UnidosFil: Song, Yuyu. Harvard Medical School; Estados UnidosFil: Jungbauer, Lisa M.. University of Illinois at Chicago; Estados UnidosFil: LaDu, Mary J.. University of Illinois at Chicago; Estados UnidosFil: Bisbal, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Lorenzo, Alfredo Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Ma, Jiyan. Van Andel Research Institute; Estados UnidosFil: Helguera, Pablo Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Morfini, Gerardo Andres. University of Illinois at Chicago; Estados UnidosFil: Brady, Scott T.. University of Illinois at Chicago; Estados UnidosFil: Pigino, Gustavo Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina. University of Illinois at Chicago; Estados UnidosPublic Library of Science2017-12-20info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/64239Zamponi, Emiliano; Buratti, Fiamma; Cataldi, Gabriel Enrique; Caicedo, Hector Hugo; Song, Yuyu; et al.; Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2; Public Library of Science; Plos One; 12; 12; 20-12-2017; 1-241932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0188340info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0188340info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:14:17Zoai:ri.conicet.gov.ar:11336/64239instacron: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:34982025-09-29 10:14:17.615CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 |
title |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 |
spellingShingle |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 Zamponi, Emiliano Fast axonal transport Prion protein Casein kinase 2 (CK2) Neuropathies |
title_short |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 |
title_full |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 |
title_fullStr |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 |
title_full_unstemmed |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 |
title_sort |
Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2 |
dc.creator.none.fl_str_mv |
Zamponi, Emiliano Buratti, Fiamma Cataldi, Gabriel Enrique Caicedo, Hector Hugo Song, Yuyu Jungbauer, Lisa M. LaDu, Mary J. Bisbal, Mariano Lorenzo, Alfredo Guillermo Ma, Jiyan Helguera, Pablo Rodolfo Morfini, Gerardo Andres Brady, Scott T. Pigino, Gustavo Fernando |
author |
Zamponi, Emiliano |
author_facet |
Zamponi, Emiliano Buratti, Fiamma Cataldi, Gabriel Enrique Caicedo, Hector Hugo Song, Yuyu Jungbauer, Lisa M. LaDu, Mary J. Bisbal, Mariano Lorenzo, Alfredo Guillermo Ma, Jiyan Helguera, Pablo Rodolfo Morfini, Gerardo Andres Brady, Scott T. Pigino, Gustavo Fernando |
author_role |
author |
author2 |
Buratti, Fiamma Cataldi, Gabriel Enrique Caicedo, Hector Hugo Song, Yuyu Jungbauer, Lisa M. LaDu, Mary J. Bisbal, Mariano Lorenzo, Alfredo Guillermo Ma, Jiyan Helguera, Pablo Rodolfo Morfini, Gerardo Andres Brady, Scott T. Pigino, Gustavo Fernando |
author2_role |
author author author author author author author author author author author author author |
dc.subject.none.fl_str_mv |
Fast axonal transport Prion protein Casein kinase 2 (CK2) Neuropathies |
topic |
Fast axonal transport Prion protein Casein kinase 2 (CK2) Neuropathies |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Prion diseases include a number of progressive neuropathies involving conformational changes in cellular prion protein (PrPc) that may be fatal sporadic, familial or infectious. Pathological evidence indicated that neurons affected in prion diseases follow a dying-back pattern of degeneration. However, specific cellular processes affected by PrPc that explain such a pattern have not yet been identified. Results from cell biological and pharmacological experiments in isolated squid axoplasm and primary cultured neurons reveal inhibition of fast axonal transport (FAT) as a novel toxic effect elicited by PrPc. Pharmacological, biochemical and cell biological experiments further indicate this toxic effect involves casein kinase 2 (CK2) activation, providing a molecular basis for the toxic effect of PrPc on FAT. CK2 was found to phosphorylate and inhibit light chain subunits of the major motor protein conventional kinesin. Collectively, these findings suggest CK2 as a novel therapeutic target to prevent the gradual loss of neuronal connectivity that characterizes prion diseases. Fil: Zamponi, Emiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Buratti, Fiamma. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Cataldi, Gabriel Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Caicedo, Hector Hugo. University of Illinois at Chicago; Estados Unidos Fil: Song, Yuyu. Harvard Medical School; Estados Unidos Fil: Jungbauer, Lisa M.. University of Illinois at Chicago; Estados Unidos Fil: LaDu, Mary J.. University of Illinois at Chicago; Estados Unidos Fil: Bisbal, Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Lorenzo, Alfredo Guillermo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Ma, Jiyan. Van Andel Research Institute; Estados Unidos Fil: Helguera, Pablo Rodolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina Fil: Morfini, Gerardo Andres. University of Illinois at Chicago; Estados Unidos Fil: Brady, Scott T.. University of Illinois at Chicago; Estados Unidos Fil: Pigino, Gustavo Fernando. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina. University of Illinois at Chicago; Estados Unidos |
description |
Prion diseases include a number of progressive neuropathies involving conformational changes in cellular prion protein (PrPc) that may be fatal sporadic, familial or infectious. Pathological evidence indicated that neurons affected in prion diseases follow a dying-back pattern of degeneration. However, specific cellular processes affected by PrPc that explain such a pattern have not yet been identified. Results from cell biological and pharmacological experiments in isolated squid axoplasm and primary cultured neurons reveal inhibition of fast axonal transport (FAT) as a novel toxic effect elicited by PrPc. Pharmacological, biochemical and cell biological experiments further indicate this toxic effect involves casein kinase 2 (CK2) activation, providing a molecular basis for the toxic effect of PrPc on FAT. CK2 was found to phosphorylate and inhibit light chain subunits of the major motor protein conventional kinesin. Collectively, these findings suggest CK2 as a novel therapeutic target to prevent the gradual loss of neuronal connectivity that characterizes prion diseases. |
publishDate |
2017 |
dc.date.none.fl_str_mv |
2017-12-20 |
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/11336/64239 Zamponi, Emiliano; Buratti, Fiamma; Cataldi, Gabriel Enrique; Caicedo, Hector Hugo; Song, Yuyu; et al.; Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2; Public Library of Science; Plos One; 12; 12; 20-12-2017; 1-24 1932-6203 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/64239 |
identifier_str_mv |
Zamponi, Emiliano; Buratti, Fiamma; Cataldi, Gabriel Enrique; Caicedo, Hector Hugo; Song, Yuyu; et al.; Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2; Public Library of Science; Plos One; 12; 12; 20-12-2017; 1-24 1932-6203 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0188340 info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0188340 |
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 |
dc.publisher.none.fl_str_mv |
Public Library of Science |
publisher.none.fl_str_mv |
Public Library of Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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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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13.070432 |