Biochemical analysis of interleukin-2 receptor beta chain phosphorylation by p56(lck).
FEBS Lett
; 447(2-3): 241-6, 1999 Mar 26.
Article
em En
| MEDLINE
| ID: mdl-10214954
ABSTRACT
Tyrosine phosphorylation of multiple proteins, including the receptor itself, is an initial event in IL-2 signaling and leads to recruitment of SH2 or PTB domain-containing proteins to the receptor. In this study, we have used subdomains of the IL-2 receptor beta chain (IL-2Rbeta) expressed in Escherichia coli as GST fusion proteins to identify the tyrosine residues that could be phosphorylated by p56(lck), one of the critical tyrosine kinases activated by IL-2. We report that recombinant p56(lck) phosphorylates in vitro tyrosine residues within the IL-2Rbeta chain but not those within the IL-2Rgamma chain. p56(lck) phosphorylates tyrosine residues 355, 358 and 361 but not 338 of the IL-2Rbeta chain acidic subdomain. Interestingly, phosphorylation of Tyr-358 appears to require the presence of either Tyr-355 or Tyr-361. p56(lck) also phosphorylates very efficiently the two tyrosines present in the IL-2Rbeta chain C-terminal region, Tyr-392 and Tyr-510. We also investigated the association of p56(lck) with the IL-2Rbeta chain which was found to depend on a short stretch of the IL-2Rbeta chain acidic subdomain, and to be independent of the presence of its tyrosine residues.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Receptores de Interleucina-2
/
Proteína Tirosina Quinase p56(lck) Linfócito-Específica
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
França