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MIP‐T3 associates with IL‐13Rα1 and suppresses STAT6 activation in response to IL‐13 stimulation
Author(s) -
Niu Yamei,
Murata Takashi,
Watanabe Ken,
Kawakami Koji,
Yoshimura Akihiko,
Inoue Jun-ichiro,
Puri Raj K,
Kobayashi Nobuyuki
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)00860-3
Subject(s) - stat6 , electrophoretic mobility shift assay , stat protein , phosphorylation , transcription factor , signal transduction , microbiology and biotechnology , receptor , activator (genetics) , chemistry , stimulation , tumor necrosis factor alpha , luciferase , biology , stat3 , biochemistry , gene , immunology , transfection , endocrinology
To unravel the mechanism of interleukin‐13 (IL‐13)‐specific functions, we sought to identify IL‐13 receptor (IL‐13R) binding molecules. A novel human IL‐13Rα1 binding protein (IL13RBP1) has been identified using yeast tri‐hybrid system, which was found to encode the same protein as MIP‐T3 (microtubule interacting protein that associates with tumor necrosis factor (TNF) receptor associating factor‐3 (TRAF3)). It constitutively associates with IL‐13Rα1 and suppresses IL‐4/13‐induced signal transducer and activator of transcription‐6 (STAT6) phosphorylation. IL‐13‐induced STAT6 activation was also inhibited as determined by dual luciferase assay and electrophoretic mobility shift assay (EMSA). These results suggest that MIP‐T3 is a novel inhibitor of IL‐13 signaling and may be a useful molecule in ameliorating various conditions in which IL‐13 plays a central role.