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Activation of the J...
Activation of the JNK pathway by distantly related protein kinases, MEKK and MUK
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- Hirai, S. (författare)
- Yokohama City University School of Medicine, Japan
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- Izawa, M. (författare)
- Yokohama City University School of Medicine, Japan
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- Osada, S. (författare)
- Yokohama City University School of Medicine, Japan
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- Spyrou, Giannis (författare)
- Karolinska Institute, Stockholm, Sweden
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- Ohno, S. (författare)
- Yokohama City University School of Medicine, Japan
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(creator_code:org_t)
- Nature Publishing Group, 1996
- 1996
- Engelska.
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Ingår i: Oncogene. - : Nature Publishing Group. - 0950-9232 .- 1476-5594. ; 12:3, s. 641-650
- Relaterad länk:
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https://urn.kb.se/re...
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http://kipublication...
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Abstract
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- 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.
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Oncogene
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