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http://hdl.handle.net/2445/118664
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DC Field | Value | Language |
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dc.contributor.author | Pérez Verdaguer, Mireia | - |
dc.contributor.author | Capera Aragonés, Jesusa | - |
dc.contributor.author | Martínez Mármol, Ramón | - |
dc.contributor.author | Camps Camprubí, Marta | - |
dc.contributor.author | Comes i Beltrán, Núria | - |
dc.contributor.author | Tamkun, Michael M. | - |
dc.contributor.author | Felipe Campo, Antonio | - |
dc.date.accessioned | 2017-12-12T16:26:51Z | - |
dc.date.available | 2017-12-12T16:26:51Z | - |
dc.date.issued | 2016-03-02 | - |
dc.identifier.issn | 2045-2322 | - |
dc.identifier.uri | http://hdl.handle.net/2445/118664 | - |
dc.description.abstract | The spatial localization of ion channels at the cell surface is crucial for their functional role. Many channels localize in lipid raft microdomains, which are enriched in cholesterol and sphingolipids. Caveolae, specific lipid rafts which concentrate caveolins, harbor signaling molecules and their targets becoming signaling platforms crucial in cell physiology. However, the molecular mechanisms involved in such spatial localization are under debate. Kv1.3 localizes in lipid rafts and participates in the immunological response. We sought to elucidate the mechanisms of Kv1.3 surface targeting, which govern leukocyte physiology. Kv1 channels share a putative caveolin-binding domain located at the intracellular N-terminal of the channel. This motif, lying close to the S1 transmembrane segment, is situated near the T1 tetramerization domain and the determinants involved in the Kvβ subunit association. The highly hydrophobic domain (FQRQVWLLF) interacts with caveolin 1 targeting Kv1.3 to caveolar rafts. However, subtle variations of this cluster, putative ancillary associations and different structural conformations can impair the caveolin recognition, thereby altering channel's spatial localization. Our results identify a caveolin-binding domain in Kv1 channels and highlight the mechanisms that govern the regulation of channel surface localization during cellular processes. | - |
dc.format.extent | 12 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Nature Publishing Group | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1038/srep22453 | - |
dc.relation.ispartof | Scientific Reports, 2016, vol. 6, p. 22453 | - |
dc.relation.uri | https://doi.org/10.1038/srep22453 | - |
dc.rights | cc-by (c) Pérez Verdaguer, Mireia et al., 2016 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es | - |
dc.source | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) | - |
dc.subject.classification | Biologia molecular | - |
dc.subject.classification | Neurociències | - |
dc.subject.other | Molecular biology | - |
dc.subject.other | Neurosciences | - |
dc.title | Caveolin interaction governs Kv1.3 lipid raft targeting | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 657501 | - |
dc.date.updated | 2017-12-12T16:26:51Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 26931497 | - |
Appears in Collections: | Articles publicats en revistes (Bioquímica i Biomedicina Molecular) Articles publicats en revistes (Institut de Biomedicina (IBUB)) Articles publicats en revistes (Biomedicina) |
Files in This Item:
File | Description | Size | Format | |
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657501.pdf | 1.42 MB | Adobe PDF | View/Open |
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