Structural interaction and functional regulation of polycystin-2 by filamin
- Autores
- Wang, Qian; Dai, Xiao-Qing; Li, Qiang; Wang, Zuocheng; Cantero, Maria del Rocio; Li, Shu; Shen, Ji; Tu, Jian-Cheng; Cantiello, Horacio Fabio; Chen, Xing-Zhen
- Año de publicación
- 2012
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Filamins are important actin cross-linking proteins implicated in scaffolding, membrane stabilization and signal transduction, through interaction with ion channels, receptors and signaling proteins. Here we report the physical and functional interaction between filamins and polycystin-2, a TRP-type cation channel mutated in 10-15% patients with autosomal dominant polycystic kidney disease. Yeast two-hybrid and GST pull-down experiments demonstrated that the C-termini of filamin isoforms A, B and C directly bind to both the intracellular N- and C-termini of polycystin-2. Reciprocal co-immunoprecipitation experiments showed that endogenous polycystin-2 and filamins are in the same complexes in renal epithelial cells and human melanoma A7 cells. We then examined the effect of filamin on polycystin-2 channel function by electrophysiology studies with a lipid bilayer reconstitution system and found that filamin-A substantially inhibits polycystin-2 channel activity. Our study indicates that filamins are important regulators of polycystin-2 channel function, and further links actin cytoskeletal dynamics to the regulation of this channel protein. © 2012 Wang et al.
Fil: Wang, Qian. University of Alberta; Canadá
Fil: Dai, Xiao-Qing. University of Alberta; Canadá
Fil: Li, Qiang. University of Alberta; Canadá
Fil: Wang, Zuocheng. University of Alberta; Canadá
Fil: Cantero, Maria del Rocio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontología. Cátedra de Biofísica; Argentina
Fil: Li, Shu. University of Alberta; Canadá
Fil: Shen, Ji. Wuhan University; China
Fil: Tu, Jian-Cheng. Wuhan University; China
Fil: Cantiello, Horacio Fabio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontología. Cátedra de Biofísica; Argentina. Massachusetts General Hospital And Harvard Medical School; Estados Unidos
Fil: Chen, Xing-Zhen. University of Alberta; Canadá - Materia
-
Polycystin-2
Filamin - 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:11336/67257
Ver los metadatos del registro completo
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Structural interaction and functional regulation of polycystin-2 by filaminWang, QianDai, Xiao-QingLi, QiangWang, ZuochengCantero, Maria del RocioLi, ShuShen, JiTu, Jian-ChengCantiello, Horacio FabioChen, Xing-ZhenPolycystin-2Filaminhttps://purl.org/becyt/ford/3.1https://purl.org/becyt/ford/3Filamins are important actin cross-linking proteins implicated in scaffolding, membrane stabilization and signal transduction, through interaction with ion channels, receptors and signaling proteins. Here we report the physical and functional interaction between filamins and polycystin-2, a TRP-type cation channel mutated in 10-15% patients with autosomal dominant polycystic kidney disease. Yeast two-hybrid and GST pull-down experiments demonstrated that the C-termini of filamin isoforms A, B and C directly bind to both the intracellular N- and C-termini of polycystin-2. Reciprocal co-immunoprecipitation experiments showed that endogenous polycystin-2 and filamins are in the same complexes in renal epithelial cells and human melanoma A7 cells. We then examined the effect of filamin on polycystin-2 channel function by electrophysiology studies with a lipid bilayer reconstitution system and found that filamin-A substantially inhibits polycystin-2 channel activity. Our study indicates that filamins are important regulators of polycystin-2 channel function, and further links actin cytoskeletal dynamics to the regulation of this channel protein. © 2012 Wang et al.Fil: Wang, Qian. University of Alberta; CanadáFil: Dai, Xiao-Qing. University of Alberta; CanadáFil: Li, Qiang. University of Alberta; CanadáFil: Wang, Zuocheng. University of Alberta; CanadáFil: Cantero, Maria del Rocio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontología. Cátedra de Biofísica; ArgentinaFil: Li, Shu. University of Alberta; CanadáFil: Shen, Ji. Wuhan University; ChinaFil: Tu, Jian-Cheng. Wuhan University; ChinaFil: Cantiello, Horacio Fabio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontología. Cátedra de Biofísica; Argentina. Massachusetts General Hospital And Harvard Medical School; Estados UnidosFil: Chen, Xing-Zhen. University of Alberta; CanadáPublic Library of Science2012-07info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/67257Wang, Qian; Dai, Xiao-Qing; Li, Qiang; Wang, Zuocheng; Cantero, Maria del Rocio; et al.; Structural interaction and functional regulation of polycystin-2 by filamin; Public Library of Science; Plos One; 7; 7; 7-2012; 40448-404501932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0040448info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0040448info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:59:19Zoai:ri.conicet.gov.ar:11336/67257instacron: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:34982025-10-15 14:59:19.33CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Structural interaction and functional regulation of polycystin-2 by filamin |
title |
Structural interaction and functional regulation of polycystin-2 by filamin |
spellingShingle |
Structural interaction and functional regulation of polycystin-2 by filamin Wang, Qian Polycystin-2 Filamin |
title_short |
Structural interaction and functional regulation of polycystin-2 by filamin |
title_full |
Structural interaction and functional regulation of polycystin-2 by filamin |
title_fullStr |
Structural interaction and functional regulation of polycystin-2 by filamin |
title_full_unstemmed |
Structural interaction and functional regulation of polycystin-2 by filamin |
title_sort |
Structural interaction and functional regulation of polycystin-2 by filamin |
dc.creator.none.fl_str_mv |
Wang, Qian Dai, Xiao-Qing Li, Qiang Wang, Zuocheng Cantero, Maria del Rocio Li, Shu Shen, Ji Tu, Jian-Cheng Cantiello, Horacio Fabio Chen, Xing-Zhen |
author |
Wang, Qian |
author_facet |
Wang, Qian Dai, Xiao-Qing Li, Qiang Wang, Zuocheng Cantero, Maria del Rocio Li, Shu Shen, Ji Tu, Jian-Cheng Cantiello, Horacio Fabio Chen, Xing-Zhen |
author_role |
author |
author2 |
Dai, Xiao-Qing Li, Qiang Wang, Zuocheng Cantero, Maria del Rocio Li, Shu Shen, Ji Tu, Jian-Cheng Cantiello, Horacio Fabio Chen, Xing-Zhen |
author2_role |
author author author author author author author author author |
dc.subject.none.fl_str_mv |
Polycystin-2 Filamin |
topic |
Polycystin-2 Filamin |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/3.1 https://purl.org/becyt/ford/3 |
dc.description.none.fl_txt_mv |
Filamins are important actin cross-linking proteins implicated in scaffolding, membrane stabilization and signal transduction, through interaction with ion channels, receptors and signaling proteins. Here we report the physical and functional interaction between filamins and polycystin-2, a TRP-type cation channel mutated in 10-15% patients with autosomal dominant polycystic kidney disease. Yeast two-hybrid and GST pull-down experiments demonstrated that the C-termini of filamin isoforms A, B and C directly bind to both the intracellular N- and C-termini of polycystin-2. Reciprocal co-immunoprecipitation experiments showed that endogenous polycystin-2 and filamins are in the same complexes in renal epithelial cells and human melanoma A7 cells. We then examined the effect of filamin on polycystin-2 channel function by electrophysiology studies with a lipid bilayer reconstitution system and found that filamin-A substantially inhibits polycystin-2 channel activity. Our study indicates that filamins are important regulators of polycystin-2 channel function, and further links actin cytoskeletal dynamics to the regulation of this channel protein. © 2012 Wang et al. Fil: Wang, Qian. University of Alberta; Canadá Fil: Dai, Xiao-Qing. University of Alberta; Canadá Fil: Li, Qiang. University of Alberta; Canadá Fil: Wang, Zuocheng. University of Alberta; Canadá Fil: Cantero, Maria del Rocio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontología. Cátedra de Biofísica; Argentina Fil: Li, Shu. University of Alberta; Canadá Fil: Shen, Ji. Wuhan University; China Fil: Tu, Jian-Cheng. Wuhan University; China Fil: Cantiello, Horacio Fabio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontología. Cátedra de Biofísica; Argentina. Massachusetts General Hospital And Harvard Medical School; Estados Unidos Fil: Chen, Xing-Zhen. University of Alberta; Canadá |
description |
Filamins are important actin cross-linking proteins implicated in scaffolding, membrane stabilization and signal transduction, through interaction with ion channels, receptors and signaling proteins. Here we report the physical and functional interaction between filamins and polycystin-2, a TRP-type cation channel mutated in 10-15% patients with autosomal dominant polycystic kidney disease. Yeast two-hybrid and GST pull-down experiments demonstrated that the C-termini of filamin isoforms A, B and C directly bind to both the intracellular N- and C-termini of polycystin-2. Reciprocal co-immunoprecipitation experiments showed that endogenous polycystin-2 and filamins are in the same complexes in renal epithelial cells and human melanoma A7 cells. We then examined the effect of filamin on polycystin-2 channel function by electrophysiology studies with a lipid bilayer reconstitution system and found that filamin-A substantially inhibits polycystin-2 channel activity. Our study indicates that filamins are important regulators of polycystin-2 channel function, and further links actin cytoskeletal dynamics to the regulation of this channel protein. © 2012 Wang et al. |
publishDate |
2012 |
dc.date.none.fl_str_mv |
2012-07 |
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/11336/67257 Wang, Qian; Dai, Xiao-Qing; Li, Qiang; Wang, Zuocheng; Cantero, Maria del Rocio; et al.; Structural interaction and functional regulation of polycystin-2 by filamin; Public Library of Science; Plos One; 7; 7; 7-2012; 40448-40450 1932-6203 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/67257 |
identifier_str_mv |
Wang, Qian; Dai, Xiao-Qing; Li, Qiang; Wang, Zuocheng; Cantero, Maria del Rocio; et al.; Structural interaction and functional regulation of polycystin-2 by filamin; Public Library of Science; Plos One; 7; 7; 7-2012; 40448-40450 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/doi/10.1371/journal.pone.0040448 info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0040448 |
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 |
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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13.22299 |