A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling.
Extracellular signal regulated kinase1/2 (ERK1/2), an important factor in signal transduction, controls cell growth, differentiation, and death. To elucidate the details of the mechanism of ERK1/2 signaling in human cells, we isolated Nef-associated factor 1 alpha (Naf1 alpha) by a yeast two-hybrid system, which bound to human ERK2. The binding ... was confirmed by a pull-down assay in vitro and immunoprecipitation in vivo. Upon EGF treatment, Naf1 alpha was phosphorylated by the EGF/MEK/ERK2 signal transduction pathway. To identify the role of Naf1 alpha in the ERK2 signaling, Naf1 alpha-expressing Saos-2 cells were analyzed for ERK2 nuclear translocation and activation of its downstream target. Overexpression of Naf1 alpha suppressed ERK2 entering into the nucleus and inhibited the ERK2-dependent Elk1-driven luciferase transcription, suggesting Naf1 alpha to be an attenuator of activated ERK2 signaling.
Mesh Terms:
Cell Nucleus, Cells, Cultured, Cytoplasm, DNA-Binding Proteins, Epidermal Growth Factor, Humans, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Mitogen-Activated Protein Kinases, Phosphorylation, Signal Transduction, Two-Hybrid System Techniques
Cell Nucleus, Cells, Cultured, Cytoplasm, DNA-Binding Proteins, Epidermal Growth Factor, Humans, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinase 3, Mitogen-Activated Protein Kinases, Phosphorylation, Signal Transduction, Two-Hybrid System Techniques
Biochem. Biophys. Res. Commun.
Date: Sep. 13, 2002
PubMed ID: 12220502
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