Tyrosine 319 in the interdomain B of ZAP-70 is a binding site for the Src homology 2 domain of Lck.
T-cell antigen receptor-induced signaling requires both ZAP-70 and Lck protein-tyrosine kinases. One essential function of Lck in this process is to phosphorylate ZAP-70 and up-regulate its catalytic activity. We have previously shown that after T-cell antigen receptor stimulation, Lck binds to ZAP-...
Hlavní autoři: | Pelosi, M, Di Bartolo, V, Mounier, V, Mège, D, Pascussi, J, Dufour, E, Blondel, A, Acuto, O |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
1999
|
Podobné jednotky
-
Role of the Src homology 2 domains and interdomain regions in ZAP-70 phosphorylation and enzymatic activity.
Autor: Magistrelli, G, a další
Vydáno: (1999) -
p56lck interacts via its src homology 2 domain with the ZAP-70 kinase.
Autor: Duplay, P, a další
Vydáno: (1994) -
Tyrosine 319, a newly identified phosphorylation site of ZAP-70, plays a critical role in T cell antigen receptor signaling.
Autor: Di Bartolo, V, a další
Vydáno: (1999) -
INTERACTION OF HUMAN P56LCK SH2 DOMAIN WITH THE ZAP-70 TYROSINE KINASE
Autor: Acuto, O, a další
Vydáno: (1994) -
INTERACTION OF SYK AND ZAP-70 WITH P56LCK/CD4
Autor: Acuto, O, a další
Vydáno: (1995)