A conserved docking motif in MAP kinases common to substrates, activators and regulators

By T. Tanoue, Makoto Adachi, T. Moriguchi, E. Nishida. Nature Cell Biology, 2000

852 citations recorded by the source corpus.

Subfields: Computational Theory and Mathematics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2fc8926faf61017a4e192277d395b43bd0d0437a

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In Computational Theory and Mathematics

1. R. Roskoski

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2. Tony Pawson
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Citations in the corpus

• Differential regulation and properties of MAPKs (2007, background): “The CD region found in ERK1/2 and JNK protein kinases is also found in p38 isoforms (Tanoue et al., 2000).”
• Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions. (2001, background): “This sequence is believed to be a putative docking site to allow D domains not only of MEK but also of other MAP kinase substrates to associate with MAP kinases (262).”
• ERK1/2 MAP kinases: structure, function, and regulation. (2012, background): “8) that contains two aspartate esidues (D318/321) previously identified as the common-docking CD) domain [106].”
• Mammalian MAPK signal transduction pathways activated by stress and inflammation: a 10-year update. (2012, background): “Importantly, the MEKK interaction motif also contains a polybasic MAPK docking site that interacts specifically with the JNK CD domain (15, 288, 289).”
• The extracellular signal-regulated kinase: Multiple substrates regulate diverse cellular functions (2006, background): “ERKs’ activation requires phosphorylation of their two regulatory residues, which are located within the MAPK’s activation motif Thr-Xaa-Tyr (Thr202, Glu203 and Tyr204 for ERK1 and Thr183, Glu184 and Tyr185 for ERK2 (Payne et al. 1991)).”
• The MEK/ERK cascade: from signaling specificity to diverse functions. (2007, background): “This region was termed initially cytoplasmic retention sequence (CRS), but was later shown important for the interaction of ERKs with many other proteins, and therefore, also termed common docking (CD) domain [50].”
• Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases (2007, background): “This KIM is proposed to interact with negatively charged aspartic acid residues (Asp316 and 319) within a common docking (CD) site identified as an essential mediator of protein–protein interactions between MAPKs and their activators, regulators and substrates (Tanoue et al., 2000).”
• Protein-protein interactions define specificity in signal transduction. (2000, background): “Remarkably, the same basic motif is found in a kinase (Mek) and phosphatase (MKP) that respectively phosphorylate and dephosphorylate Erk, suggesting that substrates and regulators may compete for the same binding site on the Erk protein kinase (Tanoue et al. 2000).”
• Mechanisms of specificity in protein phosphorylation (2007, background): “These docking domains are ubiquitous in MAPK substrate”
• ERK1/2 MAP kinases in cell survival and apoptosis (2006, background): “F aa-Xaa-F aa (where F aa represents the hydrophobic residues Leu, Ile, and possibly Val) ( 14, 16, 17 ).”