MIP-T3 associates with IL-13Rα1 and suppresses STAT6 activation in response to IL-13 stimulation

Yamei Niu; Takashi Murata; Ken Watanabe; Koji Kawakami; Akihiko Yoshimura; Jun ichiro Inoue; Raj K. Puri; Nobuyuki Kobayashi

doi:10.1016/S0014-5793(03)00860-3

MIP-T3 associates with IL-13Rα1 and suppresses STAT6 activation in response to IL-13 stimulation

Yamei Niu, Takashi Murata, Ken Watanabe, Koji Kawakami, Akihiko Yoshimura, Jun ichiro Inoue, Raj K. Puri, Nobuyuki Kobayashi

Research output: Contribution to journal › Article › peer-review

17 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	139-143
Number of pages	5
Journal	FEBS Letters
Volume	550
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(03)00860-3
Publication status	Published - 2003 Aug 28
Externally published	Yes

Keywords

Interleukin-13
Interleukin-13 receptor-α1 binding protein-1
Interleukin-4
Microtubule interacting protein that associates with tumor necrosis factor receptor associating factor-3
Signal transducer and activator of transcription-6

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(03)00860-3

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title = "MIP-T3 associates with IL-13Rα1 and suppresses STAT6 activation in response to IL-13 stimulation",

abstract = "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.",

keywords = "Interleukin-13, Interleukin-13 receptor-α1 binding protein-1, Interleukin-4, Microtubule interacting protein that associates with tumor necrosis factor receptor associating factor-3, Signal transducer and activator of transcription-6",

author = "Yamei Niu and Takashi Murata and Ken Watanabe and Koji Kawakami and Akihiko Yoshimura and Inoue, {Jun ichiro} and Puri, {Raj K.} and Nobuyuki Kobayashi",

note = "Funding Information: We acknowledge Dr. Shigeno Ohno for providing pSRHisA plasmid. We also thank Ms. Noriko Okamoto, Mr. Makoto Saito and Mrs. Yuhua Ma for technical assistance. This work was supported partly by Grant-in-Aid (for T.M.) from the Ministry of Education, Science, Technology, Sports and Culture of Japan, the Takeda Science Foundation, the Kanagawa Academy of Science and Technology, and KIHARA Memorial Yokohama Foundation for the Advancement of Life Science.",

year = "2003",

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doi = "10.1016/S0014-5793(03)00860-3",

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T1 - MIP-T3 associates with IL-13Rα1 and suppresses STAT6 activation in response to IL-13 stimulation

AU - Niu, Yamei

AU - Murata, Takashi

AU - Watanabe, Ken

AU - Kawakami, Koji

AU - Yoshimura, Akihiko

AU - Inoue, Jun ichiro

AU - Puri, Raj K.

AU - Kobayashi, Nobuyuki

N1 - Funding Information: We acknowledge Dr. Shigeno Ohno for providing pSRHisA plasmid. We also thank Ms. Noriko Okamoto, Mr. Makoto Saito and Mrs. Yuhua Ma for technical assistance. This work was supported partly by Grant-in-Aid (for T.M.) from the Ministry of Education, Science, Technology, Sports and Culture of Japan, the Takeda Science Foundation, the Kanagawa Academy of Science and Technology, and KIHARA Memorial Yokohama Foundation for the Advancement of Life Science.

PY - 2003/8/28

Y1 - 2003/8/28

N2 - 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.

AB - 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.

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KW - Interleukin-13 receptor-α1 binding protein-1

KW - Interleukin-4

KW - Microtubule interacting protein that associates with tumor necrosis factor receptor associating factor-3

KW - Signal transducer and activator of transcription-6

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JF - FEBS Letters

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ER -

MIP-T3 associates with IL-13Rα1 and suppresses STAT6 activation in response to IL-13 stimulation

Abstract

Keywords

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