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JNK‐binding protein 1 regulates NF‐κB activation through TRAF2 and TAK1
Author(s) -
Yamaguchi Tadayuki,
Miyashita Chiaki,
Koyano Satoru,
Kanda Hiromi,
Yoshioka Katsuji,
Shiba Tadayoshi,
Takamatsu Nobuhiko,
Ito Michihiko
Publication year - 2009
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2009.01.003
Subject(s) - map kinase kinase kinase , traf2 , microbiology and biotechnology , mitogen activated protein kinase kinase , mapk/erk pathway , ask1 , signal transducing adaptor protein , protein kinase a , kinase , scaffold protein , signal transduction , chemistry , biology , receptor , biochemistry , tumor necrosis factor receptor
The mitogen‐activated protein kinase (MAPK) cascades, including c‐Jun N‐terminal kinase (JNK), are composed of a MAPK, MAPK kinase (MAPKK), and MAPKK kinase (MAPKKK). Previously, we reported that JNK‐binding protein 1 (JNKBP1) enhances JNK activation induced by the TGF‐β‐activated kinase1 (TAK1) MAPKKK in transfected cells. We have investigated whether JNKBP1 functions as an adaptor protein for nuclear factor (NF)‐κB activation mediated by TAK1 in COS‐7 cells. Co‐expression experiments showed that JNKBP1 interacted with not only TAK1, but also with its upstream regulators, TNF‐receptor associated factors 2 and 6 (TRAF2 and TRAF6). An endogenous interaction between JNKBP1 and TRAF2 or TAK1 was confirmed by immunoprecipitation analysis. We also found that JNKBP1 could enhance the NF‐κB activation induced by TAK1 and TRAF2, and could promote TRAF2 polyubiquitination. These results suggest a scaffolding role for JNKBP1 in the TRAF2–TAK1–NF‐κB signaling pathway.