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dc.contributor.author
Wang, Qian
dc.contributor.author
Dai, Xiao-Qing
dc.contributor.author
Li, Qiang
dc.contributor.author
Wang, Zuocheng
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Cantero, Maria del Rocio
dc.contributor.author
Li, Shu
dc.contributor.author
Shen, Ji
dc.contributor.author
Tu, Jian-Cheng
dc.contributor.author
Cantiello, Horacio Fabio
dc.contributor.author
Chen, Xing-Zhen
dc.date.available
2019-01-02T21:25:17Z
dc.date.issued
2012-07
dc.identifier.citation
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
dc.identifier.issn
1932-6203
dc.identifier.uri
http://hdl.handle.net/11336/67257
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Public Library of Science
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Polycystin-2
dc.subject
Filamin
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Inmunología
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Medicina Básica
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CIENCIAS MÉDICAS Y DE LA SALUD
dc.title
Structural interaction and functional regulation of polycystin-2 by filamin
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-01-02T19:58:17Z
dc.journal.volume
7
dc.journal.number
7
dc.journal.pagination
40448-40450
dc.journal.pais
Estados Unidos
dc.journal.ciudad
San Francisco
dc.description.fil
Fil: Wang, Qian. University of Alberta; Canadá
dc.description.fil
Fil: Dai, Xiao-Qing. University of Alberta; Canadá
dc.description.fil
Fil: Li, Qiang. University of Alberta; Canadá
dc.description.fil
Fil: Wang, Zuocheng. University of Alberta; Canadá
dc.description.fil
Fil: Cantero, Maria del Rocio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontología. Cátedra de Biofísica; Argentina
dc.description.fil
Fil: Li, Shu. University of Alberta; Canadá
dc.description.fil
Fil: Shen, Ji. Wuhan University; China
dc.description.fil
Fil: Tu, Jian-Cheng. Wuhan University; China
dc.description.fil
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
dc.description.fil
Fil: Chen, Xing-Zhen. University of Alberta; Canadá
dc.journal.title
Plos One
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1371/journal.pone.0040448
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0040448
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