title: Endosomal clathrin drives actin accumulation at the immunological synapse.
abstract: Antigen-specific cognate interaction of T lymphocytes with antigen-presenting cells (APCs) drives major morphological and functional changes in T cells, including actin rearrangements at the immune synapse (IS) formed at the cell-cell contact area. Here we show, using cell lines as well as primary cells, that clathrin, a protein involved in endocytic processes, drives actin accumulation at the IS. Clathrin is recruited towards the IS with parallel kinetics to that of actin. Knockdown of clathrin prevents accumulation of actin and proteins involved in actin polymerization, such as dynamin-2, the Arp2/3 complex and CD2AP at the IS. The clathrin pool involved in actin accumulation at the IS is linked to multivesicular bodies that polarize to the cell-cell contact zone, but not to plasma membrane or Golgi complex. These data underscore the role of clathrin as a platform for the recruitment of proteins that promote actin polymerization at the interface of T cells and APCs.
authors.affiliation: Servicio de Inmunología, Hospital Universitario de la Princesa, Instituto de Investigación Sanitaria Hospital de la Princesa (IP), Diego de León, 62, 28006 Madrid, Spain.
authors.forename: Carmen
authors.initials: C
authors.lastname: Calabia-Linares
authors.forename: Javier
authors.initials: J
authors.lastname: Robles-Valero
authors.forename: Hortensia
authors.initials: H
authors.lastname: de la Fuente
authors.forename: Manuel
authors.initials: M
authors.lastname: Perez-Martinez
authors.forename: Noa
authors.initials: N
authors.lastname: Martín-Cofreces
authors.forename: Manuel
authors.initials: M
authors.lastname: Alfonso-Pérez
authors.forename: Cristina
authors.initials: C
authors.lastname: Gutierrez-Vázquez
authors.forename: María
authors.initials: M
authors.lastname: Mittelbrunn
authors.forename: Sales
authors.initials: S
authors.lastname: Ibiza
authors.forename: Francisco R
authors.initials: FR
authors.lastname: Urbano-Olmos
authors.forename: Covadonga
authors.initials: C
authors.lastname: Aguado-Ballano
authors.forename: Carlos Oscar
authors.initials: CO
authors.lastname: Sánchez-Sorzano
authors.forename: Francisco
authors.initials: F
authors.lastname: Sanchez-Madrid
authors.forename: Esteban
authors.initials: E
authors.lastname: Veiga
mesh_terms: D000199:Actins / Q000378:metabolism*; D000818:Animals; D000938:Antigen-Presenting Cells / Q000166:cytology / Q000276:immunology; D016764:Cell Polarity; D002478:Cells, Cultured; D002966:Clathrin / Q000235:genetics / Q000378:metabolism*; D034285:Dynamin II / Q000235:genetics / Q000378:metabolism; D056827:Endosomal Sorting Complexes Required for Transport / Q000378:metabolism; D011992:Endosomes / Q000378:metabolism*; D055785:Gene Knockdown Techniques; D006801:Humans; D054992:Immunological Synapses / Q000378:metabolism* / Q000648:ultrastructure; D019169:Jurkat Cells; D010750:Phosphoproteins / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D013601:T-Lymphocytes / Q000166:cytology / Q000276:immunology
chemical_list: D000199:Actins; D002966:Clathrin; D056827:Endosomal Sorting Complexes Required for Transport; D010750:Phosphoproteins; D011993:Recombinant Fusion Proteins; C096164:hepatocyte growth factor-regulated tyrosine kinase substrate; D034285:Dynamin II