Endosomal clathrin drives actin accumulation at the immunological synapse
| Autor: | Manuel Pérez-Martínez, Manuel Alfonso-Pérez, Carlos Oscar Sánchez-Sorzano, Hortensia de la Fuente, Francisco Sánchez-Madrid, Carmen Calabia-Linares, Noa B. Martín-Cófreces, Francisco R. Urbano-Olmos, Sales Ibiza, Esteban Veiga, Javier Robles-Valero, María Mittelbrunn, Covadonga Aguado-Ballano, Cristina Gutiérrez-Vázquez |
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| Rok vydání: | 2011 |
| Předmět: |
Immunological Synapses
Endosome Recombinant Fusion Proteins T-Lymphocytes Antigen-Presenting Cells Arp2/3 complex Endosomes macromolecular substances Clathrin Dynamin II Jurkat Cells Actin remodeling of neurons Animals Humans Cells Cultured Endosomal Sorting Complexes Required for Transport biology Cell Polarity Actin remodeling Cell Biology Phosphoproteins Actins Cell biology Gene Knockdown Techniques biology.protein Clathrin adaptor proteins MDia1 Lamellipodium |
| Zdroj: | Journal of Cell Science. 124:820-830 |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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