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Activation of the JNK pathway by distantly related protein kinases, MEKK and MUK
Yokohama City University School of Medicine, Japan.
Yokohama City University School of Medicine, Japan.
Yokohama City University School of Medicine, Japan.
Karolinska Institute, Stockholm, Sweden.
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1996 (English)In: Oncogene, ISSN 0950-9232, E-ISSN 1476-5594, Vol. 12, no 3, 641-650 p.Article in journal (Refereed) Published
Abstract [en]

JNK/SAPKs are identified as new members of the MAPK family; they phosphorylate c-Jun protein in response to several cellular stimuli including ultraviolet irradiation, TNF and osmotic shock. We have identified a protein kinase, MUK, as an activator of the JNK-pathway, whose kinase domain shows significant homology to MAPKKK-related proteins such as c-Raf and MEKK. The over-expression of MUK or MEK kinase (MEKK) in NIH3T3 or COS1 cells results in the activation of JNK1 and the accumulation of a hyper-phosphorylated form of c-Jun. While MEKK also activates the ERK pathway, MUK is a rather selective activator of the JNK pathway. On the other hand, c-Raf activates the JNK pathway only slightly despite its remarkable ability to activate the ERK pathway. Even though we originally identified MUK as a MAPKKK-related protein kinase, a greater similarity to mixed lineage kinase (MLK) is found not only in the catalytic domain but also in the 'leucine-zipper'-like motifs located at the C-terminal side of the catalytic domain. The structural divergence between MUK and MEKK reveals the multiplicity of signaling pathways that activate JNK/SAPKs.

Place, publisher, year, edition, pages
Nature Publishing Group, 1996. Vol. 12, no 3, 641-650 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:liu:diva-98850PubMedID: 8637721OAI: diva2:656001
Available from: 2013-10-14 Created: 2013-10-14 Last updated: 2013-10-22

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Spyrou, Giannis
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