Mutations which abolish phosphorylation of the TRAF-binding domain of TNF receptor 2 enhance receptor-mediated NF-kappa B activation.
Biochem Biophys Res Commun
; 244(3): 756-62, 1998 Mar 27.
Article
en En
| MEDLINE
| ID: mdl-9535738
ABSTRACT
We demonstrate that a 41 amino acid region (amino acids 379 to 419) in the cytoplasmic domain of tumor necrosis factor receptor 2 (TNFR2) is phosphorylated by unidentified kinase(s) both in vitro and in vivo. This domain (denoted x1c) corresponds almost exactly to the previously identified TRAF-binding domain and is by itself sufficient as a substrate for phosphorylation. In addition, the x1c domain is also crucial for TNFR2-mediated NF-kappa B activation. The cytoplasmic domain of TNFR2 lacks tyrosines, and conversion of all 12 potential serine and threonine phosphorylation targets in x1c to alanines either had no effect on NF-kappa B activation or resulted in enhanced NF-kappa B activity, depending on the structural context of x1c. The results show that while the TRAF-binding domain of TNFR2 is a major target of kinases, its phosphorylation is not required for NF-kappa B activation. Our data moreover suggest that phosphorylation of x1c negatively regulates the activation of NF-kappa B.
Buscar en Google
Banco de datos:
MEDLINE
Asunto principal:
Antígenos CD
/
FN-kappa B
/
Proteínas Serina-Treonina Quinasas
/
Receptores del Factor de Necrosis Tumoral
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
1998
Tipo del documento:
Article