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Protein Kinase Cδ Regulates the Depletion 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-Moreno, David; Martín, Raúl de; Quintanilla, Mario; Fernández, Teresa; Rodríguez-Silvestre, Pablo; Márquez-Expósito, Laura; Bello Gamboa, Ana; Fraile-Ramos, Alberto; Calvo, Victor ; Izquierdo, Manuel
KeywordsT lymphocytes
Immune synapse
Protein kinase C δ
Multivesicular bodies
Cytotoxic activity
Cell death
Issue Date2019
PublisherFrontiers Media
CitationImmunoPhysics and ImmunoEngineering: 370-388 (2019)
SeriesImmunoPhysics and ImmunoEngineering
AbstractMultivesicular bodies (MVB) are endocytic compartments that enclose intraluminal vesicles (ILVs) formed by inward budding from the limiting membrane of endosomes. In T lymphocytes, ILVs are secreted as Fas ligand-bearing, pro-apoptotic exosomes following T cell receptor (TCR)-induced fusion of MVB with the plasma membrane at the immune synapse (IS). In this study we show that protein kinase C δ (PKCδ), a novel PKC isotype activated by diacylglycerol (DAG), regulates TCR-controlled MVB polarization toward the IS and exosome secretion. Concomitantly, we demonstrate that PKCδ-interfered T lymphocytes are defective in activation-induced cell death. Using a DAG sensor based on the C1 DAG-binding domain of PKCδ and a GFP-PKCδ chimera, we reveal that T lymphocyte activation enhances DAG levels at the MVB endomembranes which mediates the association of PKCδ to MVB. Spatiotemporal reorganization of F-actin at the IS is inhibited in PKCδ-interfered T lymphocytes. Therefore, we propose PKCδ as a DAG effector that regulates the actin reorganization necessary for MVB traffic and exosome secretion.
Publisher version (URL)https://doi.org/10.3389/fimmu.2019.00851
Appears in Collections:(IIBM) Libros y partes de libros
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