Proceedings of the National Academy of Sciences · 2002 · 136 citations · 24 references
Life SciencesCell BiologyMolecular BiologyCell SignalingMolecular Cell BiologySignal TransductionCell Signaling NetworksCell-scaffold InteractionsProtein Kinase CascadesScaffold ProteinsSignal Transduction ComplexesJnk Signaling PathwayLeucine Zipper ProteinsMap KinasesMapk SignalingMitogen-activated Protein Kinase CascadesScaffold Protein-mediated SignalingScaffold Proteins In Signal TransductionScaffold Proteins In Signaling
Extracellular signals are transduced into cells through mitogen-activated protein kinases (MAPKs), which are activated by their upstream kinases. Recently, families of scaffolding proteins have been identified to tether specific combinations of these kinases along specific signaling pathways. Here we describe a protein, JLP (c-Jun NH2-terminal kinase-associated leucine zipper protein), which acts as a scaffolding protein to bring together Max and c-Myc along with JNK (c-Jun NH2-terminal kinase) and p38MAPK, as well as their upstream kinases MKK4 (MAPK kinase 4) and MEKK3 (MAPK kinase kinase 3). Thus, JLP defines a family of scaffolding proteins that bring MAPKs and their target transcription factors together for the execution of specific signaling pathways.
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Site-directed mutagenesis by overlap extension using the polymerase chain reaction
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