Interaction of SLP adaptors with the SH2 domain of Tec family kinases.
Eur J Immunol
; 29(11): 3702-11, 1999 11.
Article
en En
| MEDLINE
| ID: mdl-10556826
ABSTRACT
Activation of lymphocytes through their antigen receptors leads to mobilization of intracellular Ca(2+) ions. This process requires expression of SLP adaptors and involves phosphorylation of phospholipase C-gamma isoforms by the Tec-related protein tyrosine kinase Btk in B cells and Itk in T cells. The SH2 domain of Btk and Itk is essential for phospholipase C-gamma phosphorylation and mutations in this domain lead to the X-linked agammaglobulinemia immuno deficiency in humans. Here we show that, in contrast to SH2 domains from other signaling proteins, the Btk and Itk SH2 domains exhibit a restricted binding specificity. They bind selectively to tyrosine-phosphorylated SLP-65 and SLP-76 in activated B and T cells, respectively. Our findings suggest that Btk/Itk and phospholipase C-gamma both bind via their SH2 domain to phosphorylated SLP adaptors, and that this association is required for the activation of phospholipase C-gamma.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Fosfoproteínas
/
Proteínas Tirosina Quinasas
/
Linfocitos B
/
Receptores de Antígenos de Linfocitos B
/
Transducción de Señal
/
Proteínas Portadoras
/
Proteínas Tirosina Quinasas Receptoras
/
Dominios Homologos src
Límite:
Humans
Idioma:
En
Revista:
Eur J Immunol
Año:
1999
Tipo del documento:
Article
País de afiliación:
Alemania