Syntenin-1 and ezrin proteins link activated leukocyte cell adhesion molecule to the actin cytoskeleton.

Tudor, Cicerone; te Riet, Joost; Eich, Christina; Harkes, Rolf; Smisdom, Nick; Bouhuijzen Wenger, Jessica; Ameloot, Marcel; Holt, Matthew; Kanger, Johannes S; Figdor, Carl G; Cambi, Alessandra; Subramaniam, Vinod

Tudor, Cicerone; te Riet, Joost; Eich, Christina; Harkes, Rolf; Smisdom, Nick; Bouhuijzen Wenger, Jessica; Ameloot, Marcel; Holt, Matthew; Kanger, Johannes S; Figdor, Carl G; Cambi, Alessandra; Subramaniam, Vinod.

Afiliación

Tudor C; From the Nanobiophysics, MIRA Institute for Biomedical Technology and Technical Medicine and MESA+ Institute for Nanotechnology, University of Twente, 7500AE Enschede, The Netherlands.

J Biol Chem ; 289(19): 13445-60, 2014 May 09.

Article en En | MEDLINE | ID: mdl-24662291

RESUMEN

Activated leukocyte cell adhesion molecule (ALCAM) is a type I transmembrane protein member of the immunoglobulin superfamily of cell adhesion molecules. Involved in important pathophysiological processes such as the immune response, cancer metastasis, and neuronal development, ALCAM undergoes both homotypic interactions with other ALCAM molecules and heterotypic interactions with the surface receptor CD6 expressed at the T cell surface. Despite biochemical and biophysical evidence of a dynamic association between ALCAM and the actin cytoskeleton, no detailed information is available about how this association occurs at the molecular level. Here, we exploit a combination of complementary microscopy techniques, including FRET detected by fluorescence lifetime imaging microscopy and single-cell force spectroscopy, and we demonstrate the existence of a preformed ligand-independent supramolecular complex where ALCAM stably interacts with actin by binding to syntenin-1 and ezrin. Interaction with the ligand CD6 further enhances these multiple interactions. Altogether, our results propose a novel biophysical framework to understand the stabilizing role of the ALCAM supramolecular complex engaged to CD6 during dendritic cell-T cell interactions and provide novel information on the molecular players involved in the formation and signaling of the immunological synapse at the dendritic cell side.

Asunto(s)

Citoesqueleto de Actina/metabolismo; Antígenos CD/metabolismo; Moléculas de Adhesión Celular Neuronal/metabolismo; Comunicación Celular/fisiología; Proteínas del Citoesqueleto/metabolismo; Células Dendríticas/metabolismo; Proteínas Fetales/metabolismo; Sinteninas/metabolismo; Linfocitos T/metabolismo; Citoesqueleto de Actina/genética; Animales; Antígenos CD/genética; Antígenos de Diferenciación de Linfocitos T/genética; Antígenos de Diferenciación de Linfocitos T/metabolismo; Moléculas de Adhesión Celular Neuronal/genética; Proteínas del Citoesqueleto/genética; Células Dendríticas/citología; Proteínas Fetales/genética; Humanos; Células K562; Ratones; Unión Proteica; Sinteninas/genética; Linfocitos T/citología

Palabras clave

ALCAM; Actin; Atomic Force Microscopy; Cell Adhesion; Cytoskeleton; FRET-FLIM; Fluorescence Resonance Energy Transfer (FRET); Single-cell Force Spectroscopy

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Células Dendríticas / Citoesqueleto de Actina / Linfocitos T / Antígenos CD / Moléculas de Adhesión Celular Neuronal / Comunicación Celular / Proteínas del Citoesqueleto / Sinteninas / Proteínas Fetales Límite: Animals / Humans Idioma: En Revista: J Biol Chem Año: 2014 Tipo del documento: Article País de afiliación: Países Bajos Pais de publicación: Estados Unidos

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