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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.

Pubmed ID: 12220502

Authors

  • Zhang S
  • Fukushi M
  • Hashimoto S
  • Gao C
  • Huang L
  • Fukuyo Y
  • Nakajima T
  • Amagasa T
  • Enomoto S
  • Koike K
  • Miura O
  • Yamamoto N
  • Tsuchida N

Journal

Biochemical and biophysical research communications

Publication Data

September 13, 2002

Associated Grants

None

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