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Titolo:
Regulation of Cbl molecular interactions by the co-receptor molecule CD43 in human T cells
Autore:
Pedraza-Alva, G; Sawasdikosol, S; Liu, YC; Merida, LB; Cruz-Munoz, ME; Oceguera-Yanez, F; Burakoff, SJ; Rosenstein, Y;
Indirizzi:
UNAM, Inst Biotecnol, Cuernavaca 62250, Morelos, Mexico UNAM Cuernavaca Morelos Mexico 62250 l, Cuernavaca 62250, Morelos, Mexico Dana Farber Canc Inst, Boston, MA 02115 USA Dana Farber Canc Inst Boston MA USA 02115 Canc Inst, Boston, MA 02115 USA La Jolla Inst Allergy & Immunol, San Diego, CA 92121 USA La Jolla Inst Allergy & Immunol San Diego CA USA 92121 iego, CA 92121 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 1, volume: 276, anno: 2001,
pagine: 729 - 737
SICI:
0021-9258(20010105)276:1<729:ROCMIB>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOTYROSINE-BINDING DOMAIN; PROTEIN-KINASE-C; GROWTH-FACTOR RECEPTOR; PROTOONCOGENE PRODUCT; TYROSINE PHOSPHORYLATION; SIGNAL-TRANSDUCTION; PHOSPHATIDYLINOSITOL 3-KINASE; MONOCLONAL-ANTIBODY; NEGATIVE REGULATOR; ANTIGEN RECEPTOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
96
Recensione:
Indirizzi per estratti:
Indirizzo: Rosenstein, Y UNAM, Inst Biotecnol, APDO Postal 510-3, Cuernavaca 62250, Morelos, Mexico UNAM APDO Postal 510-3 Cuernavaca Morelos Mexico 62250 exico
Citazione:
G. Pedraza-Alva et al., "Regulation of Cbl molecular interactions by the co-receptor molecule CD43 in human T cells", J BIOL CHEM, 276(1), 2001, pp. 729-737

Abstract

CD43, one of the most abundant glycoproteins on the T cell surface, has been implicated in selection and maturation of thymocytes and migration, adhesion, and activation of mature T cells. The adapter molecule Cbl has been shown to be a negative regulator of Pas, Furthermore, it may also regulate intracellular signaling through the formation of several multi-molecular complexes. Here we investigated the role of Cbl in the CD43-mediated signalingpathway in human T cells. Unlike T cell receptor signaling, the interaction of the adapter protein Cbl with Vav and phosphatidylinositol 3-kinase, resulting from CD QS-specific signals, is independent of Cbl tyrosine phosphorylation, suggesting an alternative mechanism of interaction. CD43 signals induced a Cbl serine phosphorylation-dependent interaction with the tau -isoform of 14-3-3. protein. Protein kinase C-mediated Cbl serine phosphorylation was required for this interaction, because the PKC inhibitor RO-31-8220prevented it, as well as 14-3-3 dimerization. Moreover, mutation of Cbl serine residues 619, 623, 639, and 642 abolished the interaction between Cbl and 14-3-3, Overexpression of Cbl in Jurkat cells inhibited the CD43-dependent activation of the mitogen-activated protein kinase (MAPK) pathway and AP-1 transcriptional activity, confirming nevertheless a negative role for Cbl in T cell signaling. However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway. These data suggest that by inducing its phosphorylation on serine residues, CD43-mediated signals may regulate the molecular associations and functions of the Cbl adapter protein.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 10:11:59