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PROTEIN KINASE C δ REGULATES THE CLEARANCE OF ACTIN AT THE IMMUNOLOGICAL SYNAPSE REQUIRED FOR POLARIZED EXOSOME SECRETION BY T CELLS

AutorGonzalo Herranz, Pablo Aguilera, Sergio Dávila, Alicia Sánchez, Bianca Stancu, Jesús Gómez, David Fernández, Raúl de Martín, Mario Quintanilla, Teresa Fernández, Pablo Rodríguez, Vicor Calvo, Manuel Izquierdo
Palabras claveLinfocitos T, Apoptosis, AICD, Exosomas, Protein Kinase C delta, F-actin, Multivesicualr bodies
Fecha de publicación2017
ResumenMultivesicular 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.
URIhttp://hdl.handle.net/10261/159516
Aparece en las colecciones: (IIBM) Comunicaciones congresos
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