Reference work entry
Matsumoto and his colleagues discovered the kinase transforming growth factor β-activated kinase 1 (TAK1) as a new member of MAP triple kinase (MAPKKK) in 1995 using yeast complementation screening (Yamaguchi et al. 1995). TAK1 is ubiquitously expressed in all tissues and four splicing variants have been reported in human. Structurally, TAK1 has an N-terminal kinase domain and a C-terminal regulatory domain. MAPKKK is a serine/threonine-specific protein kinase involved in cellular signal transduction, where MAPKKKs phosphorylate downstream dual-specificity protein kinase MAPKKs, which in turn phosphorylates the MAPKs to regulate a variety of biological events such as cell proliferation, migration, survival, and differentiation. TAK1 has been shown to activate MAPKK3/6 and MAPKK4/7, leading to downstream...
- Inagaki M, Omori E, Kim JY, Komatsu Y, Scott G, Ray MK, Yamada G, Matsumoto K, Mishina Y, Ninomiya-Tsuji J. TAK1-binding protein 1, TAB1, mediates osmotic stress-induced TAK1 activation but is dispensable for TAK1-mediated cytokine signaling. J Biol Chem. 2008;283:33080–6.PubMedPubMedCentralCrossRefGoogle Scholar
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