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Titolo:
Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line
Autore:
Zhang, WG; Irvin, BJ; Trible, RP; Abraham, RT; Samelson, LE;
Indirizzi:
NICHHD, Cell Biol & Metab Branch, Sect Lymphocyte Signaling, NIH, Bethesda, MD 20892 USA NICHHD Bethesda MD USA 20892 ocyte Signaling, NIH, Bethesda, MD 20892 USA Mayo Clin & Mayo Fdn, Dept Immunol, Rochester, MN 55905 USA Mayo Clin & Mayo Fdn Rochester MN USA 55905 unol, Rochester, MN 55905 USA
Titolo Testata:
INTERNATIONAL IMMUNOLOGY
fascicolo: 6, volume: 11, anno: 1999,
pagine: 943 - 950
SICI:
0953-8178(199906)11:6<943:FAOLIT>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIGEN-RECEPTOR; MEMBRANE DOMAINS; TYROSINE KINASE; ACTIVATION; TRANSDUCTION; PROTEINS; PALMITOYLATION; PLC-GAMMA-1; STIMULATION; LCK;
Keywords:
LAT; TCR; tyrosine phosphorylation; palmitoylation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Samelson, LE NICHHD, Cell Biol & Metab Branch, Sect Lymphocyte Signaling, NIH, Bethesda, MD 20892 USA NICHHD Bethesda MD USA 20892 ng, NIH, Bethesda, MD 20892 USA
Citazione:
W.G. Zhang et al., "Functional analysis of LAT in TCR-mediated signaling pathways using a LAT-deficient Jurkat cell line", INT IMMUNOL, 11(6), 1999, pp. 943-950

Abstract

The adaptor molecule LAT (linker for activation of I cells) is a palmitoylated integral membrane protein that localizes to the glycolipid-enriched microdomains in the plasma membrane. Upon TCR engagement, LAT becomes phosphorylated on multiple tyrosine residues and then binds several critical signaling molecules. Here, we describe the generation and characterization of a LAT-deficient cell line, Using this cell line, we demonstrate that LAT is required for TCR-mediated Ca2+ mobilization and optimal tyrosine phosphorylation of phospholipase C-gamma 1,Vav and SLP-76, LAT is also required for Erk activation, CD69 up-regulation, and AP- and NFAT-mediated gene transcription. We also demonstrate, by reconstituting this cell line with LAT mutants, that the LAT transmembrane domain and palmitoylation at Cys26, but not Cys29, are required for LAT function and TCR signaling. These studies providefurther evidence for the crucial role of the LAT molecule, and demonstratethe use of a LAT-deficient cell line for the analysis of LAT structure andfunction.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/11/20 alle ore 22:35:23