Endosomal clathrin drives actin accumulation at the immunological synapse

[EN]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 prima...

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Detalles Bibliográficos
Autores: Calabia-Linares, Carmen, Robles Valero, Javier, de la Fuente, Hortensia, Perez-Martinez, Manuel, Martín-Cofreces, Noa, Alfonso-Pérez, Manuel, Gutierrez-Vázquez, Cristina, Mittelbrunn, María, Ibiza, Sales, Urbano-Olmos, Francisco R, Aguado-Ballano, Covadonga, Sánchez-Sorzano, Carlos Oscar, Sánchez-Madrid, Francisco, Veiga, Esteban
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2011
País:España
Institución:Universidad de Salamanca (USAL)
Repositorio:GREDOS. Repositorio Institucional de la Universidad de Salamanca
OAI Identifier:oai:gredos.usal.es:10366/168645
Acceso en línea:http://hdl.handle.net/10366/168645
Access Level:acceso abierto
Palabra clave:Immune synapse
Clathrin
Actin cytoskeleton
T cells
T-Lymphocytes
Immunological Synapses
Dynamin II
Cell Polarity
Jurkat Cells
Actins
2415 Biología Molecular
actinas
dinamina II
linfocitos T
clatrina
células Jurkat
polaridad celular
sinapsis inmunitarias
Descripción
Sumario:[EN]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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