English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/159516
logo share SHARE   Add this article to your Mendeley library MendeleyBASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Protein kinase C δ regulates the clearance of actin at the immunological synapse required for polarized exosome secretion by T cells

AuthorsHerranz, Gonzalo; Aguilera, Pablo; Dávila, Sergio; Sánchez, Alicia; Stancu, Bianca; Gómez, Jesús; Fernández, David; Martín, Raúl de; Quintanilla, Mario; Fernández, Teresa; Rodríguez, Pablo ; Calvo, Victor ; Izquierdo, Manuel
Issue Date2017
CitationEMBO Conference (2017)
AbstractMultivesicular bodies (MVB) enclose intraluminal vesicles (ILV) formed by inward budding from the membrane of endosomes. In T lymphocytes, ILV are secreted as Fas ligand-bearing, pro-apoptotic exosomes following T cell receptor (TCR)-induced fusion of the MVB with the plasma membrane at the immune synapse (IS). Diacylglycerol (DAG) and DAG kinase α (DGKα) regulate the polarized traffic of MVB towards the IS in T lymphocytes and exosome secretion. We show that Protein Kinase Cδ (PKCδ) regulates TCR-controlled, MVB polarization towards the IS and exosome secretion. Concomitantly, we demonstrate defects in activation-induced cell death in PKCδ-interfered T lymphocytes. Spatiotemporal reorganization of actin at the IS is controlled by PKCδ. TCR-controlled phosphorylation of T538 residue of adaptor paxillin at the microtubule organizing centre (MTOC) is decreased in PKCδ-interfered cells. PKCδ-dependent actin reorganization at the IS is a key regulator of MVB polarized secretory traffic.
DescriptionResumen del póster presentado a la EMBO Conference: Cell polarity and membrane dynamics, celebrada en Sant Feliu de Guixols (España) del 4 al 9 de junio de 2017.
Appears in Collections:(IIBM) Comunicaciones congresos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf59,24 kBAdobe PDFThumbnail
Show full item record
Review this work

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.