A novel Jun N‐terminal kinase (JNK)‐binding protein that enhances the activation of JNK by MEK kinase 1 and TGF‐β‐activated kinase 1

FEBS Letters

Koyano, Satoru²  Yamamoto, Ken-ichi¹  Yoshioka, Katsuji¹  Takamatsu, Nobuhiko²  Ito, Michihiko²  Shiba, Tadayoshi² 

[1] Department of Molecular Pathology, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920-0934, Japan;Department of Biosciences, School of Science, Kitasato University, 1-15-1 Kitasato, Kanagawa 228-8555, Japan

关键词: Signal transduction;    Mitogen-activated protein kinase;    Jun N-terminal kinase;    Stress-activated protein kinase;    JNK;    Jun N-terminal kinase;    SAPK;    stress-activated protein kinase;    ERK;    extracellular signal-regulated kinase;    MAPK;    mitogen-activated protein kinase;    MAPKK;    MAPK kinase;    MAPKKK;    MAPKK kinase;    MEKK1;    MEK kinase 1;    TAK1;    TGF-β-activated kinase 1;    GST;    glutathione S-transferase;   

DOI  :  10.1016/S0014-5793(99)01084-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have identified a novel Jun N-terminal kinase (JNK)-binding protein, termed JNKBP1, and examined its binding affinity for JNK1, JNK2, JNK3, and extracellular signal-regulated kinase 2 (ERK2) in COS-7 cells. JNKBP1 preferentially interacted with the JNKs, but not with ERK2. Furthermore, we investigated the effect of overexpressing JNKBP1 on the JNK and ERK signaling pathways in COS-7 cells. JNKBP1 alone had only a marginal effect on JNK activity. However, the activation of JNK by MEK kinase 1 and TGF-β-activated kinase 1 was significantly enhanced in the presence of JNKBP1. In contrast, JNKBP1 had no or very little effect on the ERK signaling pathway. These results suggest that JNKBP1 functions to facilitate the specific and efficient activation of the JNK signaling pathways.

【 授权许可】

Unknown