TY - JOUR
T1 - 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
AU - Koyano, Satoru
AU - Ito, Michihiko
AU - Takamatsu, Nobuhiko
AU - Shiba, Tadayoshi
AU - Yamamoto, Ken Ichi
AU - Yoshioka, Katsuji
N1 - Funding Information:
We thank Dr. Kunihiro Matsumoto for providing TAK1 cDNA, Yuko Odama, Norihiro Tokita and Hinako Ishizaki for technical assistance, and Dr. Yoshiyuki Sakaki for encouragement. This work was supported in part by grants from the Kitasato Research Foundation (M.I.), the Waksman Foundation of Japan Inc. (T.S.), and the Kato Memorial Foundation (K.Y.).
PY - 1999/9/3
Y1 - 1999/9/3
N2 - 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. Copyright (C) 1999 Federation of European Biochemical Societies.
AB - 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. Copyright (C) 1999 Federation of European Biochemical Societies.
KW - Jun N-terminal kinase
KW - Mitogen-activated protein kinase
KW - Signal transduction
KW - Stress-activated protein kinase
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U2 - 10.1016/S0014-5793(99)01084-4
DO - 10.1016/S0014-5793(99)01084-4
M3 - Article
C2 - 10471813
AN - SCOPUS:0032864251
SN - 0014-5793
VL - 457
SP - 385
EP - 388
JO - FEBS Letters
JF - FEBS Letters
IS - 3
ER -