Nuclear translocation of p90Rsk and phosphorylation of CREB is induced by ionomycin in a Ras-independent manner in

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Updated: Sep 29, 2026

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development
09:32

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

G Boglári1, J Szeberényi

  • 1Department of Medical Biology, Faculty of Medicine, University of Pécs, Hungary.

Acta Biologica Hungarica
|October 10, 2002
PubMed

Insights

The p90Rsk kinase plays a role in neuronal differentiation of PC12 cells, particularly when Ras protein is blocked. It may substitute for ERK pathways in nerve growth factor (NGF) and ionomycin-induced differentiation.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Neuronal differentiation is crucial for nervous system development.
  • Nerve growth factor (NGF) typically induces neuronal differentiation in PC12 cells via the Ras/MAPK/ERK pathway.
  • PC12-M17 cells with blocked Ras signaling fail to differentiate with NGF alone, but respond to NGF plus ionomycin.

Purpose of the Study:

  • To investigate the role of p90Rsk in neuronal differentiation.
  • To explore alternative signaling pathways in Ras-blocked PC12 cells.

Main Methods:

  • Utilized PC12 and PC12-M17 cells.
  • Induced differentiation with NGF and ionomycin.
  • Assessed p90Rsk nuclear translocation.
  • Measured cAMP response element binding protein (CREB) phosphorylation.

Main Results:

  • Ionomycin induced p90Rsk nuclear translocation in both cell types.
  • Nuclear p90Rsk correlated with increased CREB phosphorylation.
  • This suggests a role for p90Rsk in Ras-independent differentiation.

Conclusions:

  • p90Rsk may compensate for ERK pathway inhibition in neuronal differentiation.
  • p90Rsk could be a key kinase in Ras-independent NGF/ionomycin signaling.
  • This finding expands our understanding of neuronal differentiation signaling.

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