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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/67257

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network_name_str CONICET Digital (CONICET)
spelling 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
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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