Phosphorylation of fodrin (nonerythroid spectrin) by the purified insulin receptor kinase

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Summary

Fodrin (nonerythroid spectrin) from porcine brain was found to be phosphorylated on tyrosine residues by the purified insulin receptor kinase. The phosphorylation occurred in an insulin-sensitive manner with a physiologically relevant Km. The β (235 K) subunit of fodrin, but not the α (240 K) subunit, was phosphorylated by the kinase. Neither the α (240 K) subunit nor the β (220 K) subunit of erythrocyte spectrin was phosphorylated under the same conditions. Fodrin phosphorylation by the purified insulin receptor kinase was markedly inhibited by F-actin. These data raise the possibility that tyrosine phosphorylation of fodrin plays some roles in the regulation of plasma membrane-microfilament interaction.

References (27)

  • UshiroH. et al.

    J. Biol. Chem.

    (1980)
  • BockusB.J. et al.

    Exp. Cell Res.

    (1984)
  • GlenneyJ.R. et al.

    Cell

    (1982)
  • LazaridesE. et al.

    Cell

    (1982)
  • Fujita-YamaguchiY. et al.

    J. Biol. Chem.

    (1983)
  • DavisJ. et al.

    J. Biol. Chem.

    (1983)
  • BrennerS.L. et al.

    J. Biol. Chem.

    (1979)
  • SpudichJ.A. et al.

    J. Biol. Chem.

    (1971)
  • KasugaM. et al.

    J. Biol. Chem.

    (1983)
  • StadtmauerL.A. et al.

    J. Biol. Chem.

    (1983)
  • PikeL.J. et al.

    J. Biol. Chem.

    (1984)
  • CooperJ.A. et al.

    Current Topics in Microbiology and Immunology

    (1983)
  • EkB. et al.

    Nature

    (1982)
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