Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/57645
COMPARTIR / EXPORTAR:
logo share SHARE logo core CORE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

MAL Protein Controls Protein Sorting at the Supramolecular Activation Cluster of Human T Lymphocytes

AutorAntón, Olga M. CSIC ORCID; Andrés-Delgado, Laura CSIC ORCID; Reglero-Real, Natalia CSIC; Batista, Alicia; Alonso, Miguel A. CSIC ORCID
Palabras claveImmunological synapse
T cell membrane receptors
Supramolecular activation cluster
Jurkat T cell
Fecha de publicación25-may-2011
EditorAmerican Association of Immunologists
CitaciónJournal of Immunology 186 (11): 6345-6356 (2011)
ResumenT cell membrane receptors and signaling molecules assemble at the immunological synapse (IS) in a supramolecular activation cluster (SMAC), organized into two differentiated subdomains: the central SMAC (cSMAC), with the TCR, Lck, and linker for activation of T cells (LAT), and the peripheral SMAC (pSMAC), with adhesion molecules. The mechanism of protein sorting to the SMAC subdomains is still unknown. MAL forms part of the machinery for protein targeting to the plasma membrane by specialized mechanisms involving condensed membranes or rafts. In this article, we report our investigation of the dynamics of MAL during the formation of the IS and its role in SMAC assembly in the Jurkat T cell line and human primary T cells. We observed that under normal conditions, a pool of MAL rapidly accumulates at the cSMAC, where it colocalized with condensed membranes, as visualized with the membrane fluorescent probe Laurdan. Mislocalization of MAL to the pSMAC greatly reduced membrane condensation at the cSMAC and redistributed machinery involved in docking microtubules or transport vesicles from the cSMAC to the pSMAC. As a consequence of these alterations, the raft-associated molecules Lck and LAT, but not the TCR, were missorted to the pSMAC. MAL, therefore, regulates membrane order and the distribution of microtubule and transport vesicle docking machinery at the IS and, by doing so, ensures correct protein sorting of Lck and LAT to the cSMAC.
Versión del editorhttp://dx.doi.org/10.4049/jimmunol.1003771
URIhttp://hdl.handle.net/10261/57645
DOI10.4049/jimmunol.1003771
ISSN0022-1767
E-ISSN1550-660
Aparece en las colecciones: (CBM) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

CORE Recommender

SCOPUSTM   
Citations

51
checked on 13-mar-2024

WEB OF SCIENCETM
Citations

48
checked on 24-feb-2024

Page view(s)

313
checked on 19-mar-2024

Download(s)

101
checked on 19-mar-2024

Google ScholarTM

Check

Altmetric

Altmetric


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.