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

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-beta-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.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, COS Cells, Calcium-Calmodulin-Dependent Protein Kinases, Carrier Proteins, Cloning, Molecular, Hybrid Cells, Intracellular Signaling Peptides and Proteins, JNK Mitogen-Activated Protein Kinases, MAP Kinase Kinase Kinase 1, MAP Kinase Kinase Kinases, Mice, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, Molecular Sequence Data, Protein-Serine-Threonine Kinases, Recombinant Proteins, Signal Transduction, Transfection, Yeasts
FEBS Lett.
Date: Sep. 03, 1999
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