Biochemical analysis of interleukin‐2 receptor β chain phosphorylation by p56lck

FEBS Letters

Fagard, Remi²  Bouvier, Ghislaine¹  Bertoglio, Jacques¹  Delespine-Carmagnat, Maryvonnick¹  Allée, Guillaume² 

[1] INSERM Unit 461, Faculté de Pharmacie Paris-Xl, 5 rue Jean-Baptiste Clément, 92296 Châtenay-Malabry, France;Service de Biochimie, Hopital Avicenne, 125 route de Stalingrad, 93009 Bobigny, France

关键词: Interleukin-2 receptor;    Tyrosine phosphorylation;    IL-2;    interleukin-2;    IL-2R;    interleukin-2 receptor;    GST;    glutathione S-transferase;    SH2;    Src homology 2 domain;    PTB;    phosphotyrosine binding domain;    PTK;    protein tyrosine kinase;   

DOI  :  10.1016/S0014-5793(99)00301-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 β chain (IL-2Rβ) 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-2Rβ chain but not those within the IL-2Rγ chain. p56^lck phosphorylates tyrosine residues 355, 358 and 361 but not 338 of the IL-2Rβ 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-2Rβ chain C-terminal region, Tyr-392 and Tyr-510. We also investigated the association of p56^lck with the IL-2Rβ chain which was found to depend on a short stretch of the IL-2Rβ chain acidic subdomain, and to be independent of the presence of its tyrosine residues.

【 授权许可】

Unknown