Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/3680
COMPARTIR / EXPORTAR:
SHARE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Lck-Dependent Tyrosine Phosphorylation of Diacylglycerol Kinase {alpha} Regulates Its Membrane Association in T Cells |
Autor: | Merino Plaza, Ernesto; Ávila Flores, Juana Antonia; Shiriai, Yasuhito; Moraga, Ignacio; Saito, Naoaki; Mérida, Isabel CSIC ORCID | Fecha de publicación: | may-2008 | Citación: | J Immunol. 2008 May 1;180(9):5805-15 | Resumen: | TCR engagement triggers phospholipase Cgamma1 activation through the Lck-ZAP70-linker of activated T cell adaptor protein pathway. This leads to generation of diacylglycerol (DAG) and mobilization of intracellular Ca(2+), both essential for TCR-dependent transcriptional responses. TCR ligation also elicits transient recruitment of DAG kinase alpha (DGKalpha) to the lymphocyte plasma membrane to phosphorylate DAG, facilitating termination of DAG-regulated signals. The precise mechanisms governing dynamic recruitment of DGKalpha to the membrane have not been fully elucidated, although Ca(2+) influx and tyrosine kinase activation were proposed to be required. We show that DGKalpha is tyrosine phosphorylated, and identify tyrosine 335 (Y335), at the hinge between the atypical C1 domains and the catalytic region, as essential for membrane localization. Generation of an Ab that recognizes phosphorylated Y335 demonstrates Lck-dependent phosphorylation of endogenous DGKalpha during TCR activation and shows that pY335DGKalpha is a minor pool located exclusively at the plasma membrane. Our results identify Y335 as a residue critical for DGKalpha function and suggest a mechanism by which Lck-dependent phosphorylation and Ca(2+) elevation regulate DGKalpha membrane localization. The concerted action of these two signals results in transient, receptor-regulated DGKalpha relocalization to the site at which it exerts its function as a negative modulator of DAG-dependent signals. | URI: | http://hdl.handle.net/10261/3680 | ISBN: | PMID: 18424699 |
Aparece en las colecciones: | (CNB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
proof-3.pdf | 711,15 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
PubMed Central
Citations
17
checked on 20-abr-2024
SCOPUSTM
Citations
33
checked on 20-abr-2024
WEB OF SCIENCETM
Citations
23
checked on 27-feb-2024
Page view(s)
321
checked on 24-abr-2024
Download(s)
269
checked on 24-abr-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.