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dc.contributor.author Rodríguez Walker, Macarena
dc.contributor.author Vilcaes, Aldo Alejandro
dc.contributor.author Garbarino Pico, Eduardo
dc.contributor.author Daniotti, Jose Luis
dc.date.available 2018-07-02T13:45:05Z
dc.date.issued 2015-08
dc.identifier.citation Rodríguez Walker, Macarena; Vilcaes, Aldo Alejandro; Garbarino Pico, Eduardo; Daniotti, Jose Luis; Role of plasma-membrane-bound sialidase NEU3 in clathrin-mediated endocytosis; Portland Press; Biochemical Journal; 470; 1; 8-2015; 131-144
dc.identifier.issn 0264-6021
dc.identifier.uri http://hdl.handle.net/11336/50815
dc.description.abstract Gangliosides are sialic acid-containing glycosphingolipids mainly expressed at the outer leaflet of the plasma membrane. Sialidase NEU3 is a key enzyme in the catabolism of gangliosides with its up-regulation having been observed in human cancer cells. In the case of CME (clathrin-mediated endocytosis), although this has been widely studied, the role of NEU3 and gangliosides in this cellular process has not yet been established. In the present study, we found an increased internalization of Tf (transferrin), the archetypical cargo for CME, in cells expressing complex gangliosides with high levels of sialylation. The ectopic expression of NEU3 led to a drastic decrease in Tf endocytosis, suggesting the participation of gangliosides in this process. However, the reduction in Tf endocytosis caused by NEU3 was still observed in glycosphingolipid-depleted cells, indicating that NEU3 could operate in a way that is independent of its action on gangliosides. Additionally, internalization of α2-macroglobulin and low-density lipoprotein, other typical ligands in CME, was also decreased in NEU3-expressing cells. In contrast, internalization of cholera toxin β-subunit, which is endocytosed by both clathrin-dependent and clathrin-independent mechanisms, remained unaltered. Kinetic assays revealed that NEU3 caused a reduction in the sorting of endocytosed Tf to early and recycling endosomes, with the Tf binding at the cell surface being also reduced. NEU3-expressing cells showed an altered subcellular distribution of clathrin adaptor AP-2 (adaptor protein 2), but did not reveal any changes in the membrane distribution of clathrin, PtdIns(4,5)P2 or caveolin-1. Overall, these results suggest a specific and novel role of NEU3 in CME.
dc.format application/pdf
dc.language.iso eng
dc.publisher Portland Press
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights Atribución-NoComercial-CompartirIgual 2.5 Argentina (CC BY-NC-SA 2.5 AR)
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject CLATHRIN
dc.subject GANGLIOSIDE
dc.subject GLYCOLIPID
dc.subject MEMBRANE TRAFFICKING
dc.subject NEU3
dc.subject SIALIDASE
dc.subject.classification Otras Ciencias Biológicas
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title Role of plasma-membrane-bound sialidase NEU3 in clathrin-mediated endocytosis
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2018-06-29T16:43:51Z
dc.identifier.eissn 1470-8728
dc.journal.volume 470
dc.journal.number 1
dc.journal.pagination 131-144
dc.journal.pais Reino Unido
dc.journal.ciudad Londres
dc.description.fil Fil: Rodríguez Walker, Macarena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil Fil: Vilcaes, Aldo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil Fil: Garbarino Pico, Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.description.fil Fil: Daniotti, Jose Luis. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
dc.journal.title Biochemical Journal
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1042/BJ20141550
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/http://www.biochemj.org/content/470/1/131
dc.conicet.fuente unificacion


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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)