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Titolo:
Dual fatty acylation of p59(Fyn) is required for association with the T cell receptor zeta chain through phosphotyrosine Src homology domain-2 interactions
Autore:
vant Hof, W; Resh, MD;
Indirizzi:
Mem Sloan Kettering Canc Ctr, Cell Biol Program, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 2, volume: 145, anno: 1999,
pagine: 377 - 389
SICI:
0021-9525(19990419)145:2<377:DFAOPI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-TYROSINE KINASE; AMINO-TERMINAL DOMAIN; PLASMA-MEMBRANE; N-MYRISTOYLTRANSFERASE; ANTIGEN-RECEPTOR; MYRISTIC ACID; V-SRC; ACTIVATION; MOTIF; PALMITOYLATION;
Keywords:
Src homology domains; acylation; cell membrane; protein-tyrosine kinase; receptor/antigen;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Resh, MD Mem Sloan Kettering Canc Ctr, Cell Biol Program, 1275 York Ave,Box 143, New Mem Sloan Kettering Canc Ctr 1275 York Ave,Box 143 New York NY USA 10021
Citazione:
W. van't Hof e M.D. Resh, "Dual fatty acylation of p59(Fyn) is required for association with the T cell receptor zeta chain through phosphotyrosine Src homology domain-2 interactions", J CELL BIOL, 145(2), 1999, pp. 377-389

Abstract

The first 10 residues within the Src homology domain (SH)-4 domain of the Src family kinase Fyn are required for binding to the immune receptor tyrosine-based activation motif (ITAM) of T cell receptor (TCR) subunits. Recently, mutation of glycine 2, cysteine 3, and lysines 7 and 9 was shown to block binding of Fyn to TCR zeta chain ITAMs, prompting the designation of these residues as an ITAM recognition motif (Gauen, L.K.T., M,E. Linder, and A,S. Shaw. 1996. J, Cell Biol, 133:1007-1015), Here we show that these residues do not mediate direct interactions with TCR ITAMs, but rather are required for efficient myristoylation and palmitoylation of Fyn, Specifically, coexpression of a K(7,9)A-Fyn mutant with N-myristoyltransferase restored myristoylation, membrane binding, and association with the cytoplasmic tail of TCR zeta fused to CD8, Conversely, treatment of cells with 2-hydroxymyristate, a myristoylation inhibitor, blocked association of wildtype Fyn with zeta. The Fyn NH2 terminus was necessary but not sufficient for interactionwith zeta and both Fyn kinase and SH2 domains were required, directing phosphorylation of zeta ITAM tyrosines and binding to zeta ITAM phosphotyrosines. Fyn/zeta interaction was sensitive to octylglucoside and filipin, agents that disrupt membrane rafts. Moreover, a plasma membrane bound, farnesylated Fyn construct, G(2)A,C3S-FynKRas, was not enriched in the detergent insoluble fraction and did not associate with zeta. We conclude that the Fyn SH4 domain provides the signals for fatty acylation and specific plasma membrane localization, stabilizing the interactions between the Fyn SH2 domain and phosphotyrosines in TCR zeta chain ITAMs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 22:31:37