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The phosphorylation of stathmin by MAP kinase

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Reversible Protein Phosphorylation in Cell Regulation

Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 11))

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Abstract

Stathmin, a ubiquitous cytosolic phosphoprotein 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 stoichio-metrically 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. (Mol Cell Biochem 127/128: 151–156, 1993)

Submitted February 1993.

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Authors and Affiliations

  1. MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee, DD14HN, Scotland, UK

    Ian A. Leighton, David G. Campbell & Philip Cohen

  2. INSERM U153-CNRS URA614, 17 rue du Fer a Moulin, 75005, Paris, France

    Patrick Curmi & Andre Sobel

Authors
  1. Ian A. Leighton
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  2. Patrick Curmi
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  3. David G. Campbell
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  4. Philip Cohen
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  5. Andre Sobel
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan, Canada, S7N 0W0

    R. L. Khandelwal

  2. Department of Medical Biochemistry, University of Calgary, Health Science Centre, 3330 Hospital Drive N.W., Calgary, Alberta, Canada, TZN 4N1

    J. H. Wang

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© 1993 Kluwer Academic Publishers

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Leighton, I.A., Curmi, P., Campbell, D.G., Cohen, P., Sobel, A. (1993). The phosphorylation of stathmin by MAP kinase. In: Khandelwal, R.L., Wang, J.H. (eds) Reversible Protein Phosphorylation in Cell Regulation. Developments in Molecular and Cellular Biochemistry, vol 11. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2600-1_14

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  • DOI: https://doi.org/10.1007/978-1-4615-2600-1_14

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-7923-2637-3

  • Online ISBN: 978-1-4615-2600-1

  • eBook Packages: Springer Book Archive

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