Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/288721
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | A proteomic analysis reveals the interaction of GluK1 ionotropic kainate receptor subunits with go proteins |
Autor: | Rutkowska-Wlodarczyk, Izabela CSIC; Aller, María Isabel CSIC ORCID; Valbuena, Sergio CSIC ORCID; Bologna, Jean-Charles; Prézeau, Laurent; Lerma Gómez, Juan CSIC ORCID | Palabras clave: | GluK1 Go protein Kainate receptors Metabotropic Noncanonical Proteomics |
Fecha de publicación: | 2015 | Editor: | Society for Neuroscience | Citación: | Journal of Neuroscience 35(13): 5171-5179 (2015) | Resumen: | Kainate receptors (KARs) are found ubiquitously in the CNS and are present presynaptically and postsynaptically regulating synaptic transmission and excitability. Functional studies have proven that KARs act as ion channels as well as potentially activating G-proteins, thus indicating the existance of a dual signaling system for KARs. Nevertheless, it is not clear how these ion channels activate G-proteins and which of the KAR subunits is involved. Here we performed a proteomic analysis to define proteins that interact with the C-terminal domain of GluK1 and we identified a variety of proteins with many different functions, including a Go α subunit. These interactions were verified through distinct in vitro and in vivo assays, and the activation of the Go protein by GluK1 was validated in bioluminescence resonance energy transfer experiments, while the specificity of this association was confirmed in GluK1-deficient mice. These data reveal components of the KAR interactome, and they show that GluK1 and Go proteins are natural partners, accounting for the metabotropic effects of KARs. | Versión del editor: | https://doi.org/10.1523/JNEUROSCI.5059-14.2015 | URI: | http://hdl.handle.net/10261/288721 | DOI: | 10.1523/JNEUROSCI.5059-14.2015 | E-ISSN: | 1529-2401 |
Aparece en las colecciones: | (IN) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
proteoprotei.pdf | 1,24 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
10
checked on 27-mar-2024
SCOPUSTM
Citations
18
checked on 09-may-2024
WEB OF SCIENCETM
Citations
17
checked on 26-feb-2024
Page view(s)
30
checked on 15-may-2024
Download(s)
20
checked on 15-may-2024
Google ScholarTM
Check
Altmetric
Altmetric
Artículos relacionados:
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.