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• W2034247990 abstract "The c-Jun N-terminal kinase (JNK) signaling pathway is a major mediator of stress responses in cells. Similar to other mitogen-activated protein kinases (MAPKs), JNK activity is controlled by a cascade of protein kinases and by protein phosphatases, including dual-specificity MAPK phosphatases. Components of the JNK pathway associate with scaffold proteins that modulate their activities and cellular localization. The JNK-interacting protein-1 (JIP-1) scaffold protein specifically binds JNK, MAPK kinase 7 (MKK7), and members of the mixed lineage kinase (MLK) family, and regulates JNK activation in neurons. In this study we demonstrate that distinct regions within the N termini of MKK7 and the MLK family member dual leucine zipper kinase (DLK) mediate their binding to JIP-1. We have also identified amino acids in JNK required for: (a) binding to JIP-1 and for JIP-1-mediated JNK activation, (b) docking to MAPK kinase 4 (MKK4) and efficient phosphorylation by MKK4, and (c) docking to its substrate c-Jun and efficient c-Jun phosphorylation. None of the amino acids identified were essential for JNK docking to MKK7 or the dual-specificity phosphatase MAPK phosphatase 7 (MKP7). These findings uncover molecular determinants of JIP-1 scaffold complex assembly and demonstrate that there are overlapping, but also distinct, binding determinants within JNK that mediate interactions with scaffold proteins, activators, phosphatases, and substrates." @default.
• W2034247990 created "2016-06-24" @default.
• W2034247990 creator A5058970955 @default.
• W2034247990 creator A5078982842 @default.
• W2034247990 date "2004-03-01" @default.
• W2034247990 modified "2023-09-29" @default.
• W2034247990 title "Docking Interactions in the c-Jun N-terminal Kinase Pathway" @default.
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• W2034247990 doi "https://doi.org/10.1074/jbc.m311841200" @default.
• W2034247990 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14699111" @default.
• W2034247990 hasPublicationYear "2004" @default.
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