Endosomal clathrin drives actin accumulation at the immunological synapse

• DOI: 10.1242/jcs.078832
• Publication Date: 2011-02-15T06:06:18Z
• Authors: Carmen Calabia-Li...; Javier Robles-Valero; Hortensia de la F...; Manuel Perez-Mart...; Noa Martín-Cofreces; Manuel Alfonso-Pérez; Cristina Gutierre...; María Mittelbrunn; Sales Ibiza; Francisco R. Urba...; Covadonga Aguado-...; Carlos Oscar Sánc...; Francisco Sanchez...; Esteban Veiga
• Keywords: 0301 basic medicine; Endosomal Sorting Complexes Required for Transport; Immunological Synapses; Recombinant Fusion Proteins; T-Lymphocytes; Antigen-Presenting Cells; Cell Polarity; Endosomes; Phosphoproteins; Actins; Clathrin; Dynamin II; Jurkat Cells; 03 medical and health sciences; Gene Knockdown Techniques; Animals; Humans; Cells, Cultured

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.