Brain-derived neurotrophic factor stimulates phosphorylation of stathmin in cortical neurons

Jean René Cardinaux, Pierre Magistretti, Jean Luc Martin*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


We have identified by two-dimensional polyacrylamide gel electrophoresis a protein known as stathmin which is phosphorylated in a time- and concentration-dependent manner in response to brain-derived neurotrophic factor (BDNF) in primary cultures of cortical neurons. We show that stathmin phosphorylation is preceded by the activation of mitogen-activated protein kinase (MAPK) isoforms p44 and p42. Moreover, the MAPK kinase inhibitor PD 098059, which inhibits MAPK activation, also markedly reduces BDNF-stimulated phosphorylation of stathmin, therefore suggesting that phosphorylation of stathmin is triggered by the activation of MAPK. Phosphorylation of stathmin is specific for BDNF since nerve growth factor does not stimulate MAPK and stathmin phosphorylation in cultured cortical neurons. Taken together, these results identify stathmin as a new target protein of BDNF, possibly involved in the development of cortical neurons.

Original languageEnglish (US)
Pages (from-to)220-228
Number of pages9
JournalMolecular Brain Research
Issue number1-2
StatePublished - Nov 1 1997


  • 2D-PAGE
  • Brain-derived neurotrophic factor (BDNF)
  • Cortical neurons
  • Mitogen-activated protein kinase (MAPK)
  • Nerve growth factor (NGF)
  • Phosphorylation
  • Stathmin

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience

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