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dc.contributor.author
Cantero, Maria del Rocio
dc.contributor.author
Cantiello, Horacio Fabio
dc.date.available
2018-03-13T21:09:40Z
dc.date.issued
2015-05
dc.identifier.citation
Cantero, Maria del Rocio; Cantiello, Horacio Fabio; Polycystin-2 (TRPP2) regulation by Ca2+ is effected and diversified by actin-binding proteins; Cell Press; Biophysical Journal; 108; 9; 5-2015; 2191-2200
dc.identifier.issn
0006-3495
dc.identifier.uri
http://hdl.handle.net/11336/38725
dc.description.abstract
Calcium regulation of Ca2+-permeable ion channels is an important mechanism in the control of cell function. Polycystin-2 (PC2, TRPP2), a member of the transient receptor potential superfamily, is a nonselective cation channel with Ca2+ permeability. The molecular mechanisms associated with PC2 regulation by Ca2+ remain ill-defined. We recently demonstrated that PC2 from human syncytiotrophoblast (PC2hst) but not the in vitro translated protein (PC2iv), functionally responds to changes in intracellular (cis) Ca2+. In this study we determined the regulatory effect(s) of Ca2+-sensitive and -insensitive actin-binding proteins (ABPs) on PC2iv channel function in a lipid bilayer system. The actin-bundling protein α-actinin increased PC2iv channel function in the presence of cis Ca2+, although instead was inhibitory in its absence. Conversely, filamin that shares actin-binding domains with α-actinin had a strong inhibitory effect on PC2iv channel function in the presence, but no effect in the absence of cis Ca2+. Gelsolin stimulated PC2iv channel function in the presence, but not the absence of cis Ca2+. In contrast, profilin that shares actin-binding domains with gelsolin, significantly increased PC2iv channel function both in the presence and absence of Ca2+. The distinct effect(s) of the ABPs on PC2iv channel function demonstrate that Ca2+ regulation of PC2 is actually mediated by direct interaction(s) with structural elements of the actin cytoskeleton. These data indicate that specific ABP-PC2 complexes would confer distinct Ca2+-sensitive properties to the channel providing functional diversity to the cytoskeletal control of transient receptor potential channel regulation.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Cell Press
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
Actin-Binding Proteins
dc.subject.classification
Otras Ciencias Biológicas
dc.subject.classification
Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Polycystin-2 (TRPP2) regulation by Ca2+ is effected and diversified by actin-binding proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-13T13:58:00Z
dc.journal.volume
108
dc.journal.number
9
dc.journal.pagination
2191-2200
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Cantero, Maria del Rocio. Universidad de Buenos Aires. Facultad de Odontologia. Cátedra de Biofísica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Cantiello, Horacio Fabio. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad de Buenos Aires. Facultad de Odontologia. Cátedra de Biofísica; Argentina
dc.journal.title
Biophysical Journal
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bpj.2015.03.050
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0006349515003380
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