The phosphorylation of stathmin by MAP kinase

Ian A. Leighton, Patrick Curmi, David G. Campbell, Philip Cohen, Andre Sobel

Research output: Contribution to journalArticlepeer-review

69 Citations (Scopus)


Stathmin, a ubiquitous cytosolic phosphoprotei which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF.

Original languageEnglish
Pages (from-to)151-156
Number of pages6
JournalMolecular and Cellular Biochemistry
Issue number1
Publication statusPublished - 1 Nov 1993


  • MAP kinase
  • nerve growth factor
  • PC12 cells
  • protein kinase
  • stathmin

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology


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