作者: Daniel H. Kaplan , Andrew C. Greenlund , J. William Tanner , Andrey S. Shaw , Robert D. Schreiber
DOI: 10.1074/JBC.271.1.9
关键词:
摘要: We have shown previously that a four-amino acid block residing at positions 266-269 (LPKS) in the intracellular domain of human interferon-γ (IFN-γ) receptor α chain is critical for IFN-γ-dependent tyrosine kinase activation and biologic response induction. Herein we show this sequence required constitutive attachment JAK-1. Using vaccinia expression system, chain-specific monoclonal antibody coprecipitated JAK-1 from cells coexpressing either (a) wild type IFN-γ chain, (b) truncation mutant containing only first 59 amino acids, or (c) alanine substitutions functionally irrelevant residues 272-275. In contrast, was not when coexpressed with (LPKS). Mutagenesis LPKS revealed Pro-267 residue obligatorily function. addition, binding. These results thus identify site association establish signal transduction.