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Endosomal clathrin drives actin accumulation at the immunological synapse
Author(s) -
Carmen Calabia-Linares,
Javier RoblesValero,
Hortensia de la Fuente,
Manuel PérezMartínez,
Noa B. MartínCófreces,
Manuel Alfonso-Pérez,
Cristina GutiérrezVázquez,
Marı́a Mittelbrunn,
Sales Ibiza,
Francisco R. Urbano-Olmos,
Covadonga Aguado-Ballano,
Carlos Óscar S. Sorzano,
Francisco SánchezMadrid,
Esteban Veiga
Publication year - 2011
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.078832
Subject(s) - clathrin , microbiology and biotechnology , biology , endocytic cycle , dynamin , immunological synapse , endosome , actin , actin remodeling of neurons , actin remodeling , actin binding protein , endocytosis , actin cytoskeleton , t cell , cell , cytoskeleton , t cell receptor , immune system , immunology , biochemistry , intracellular
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.

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