Phosphorylation of hepatic insulin receptor by casein kinase 2

Jorge Grande, Mercè Pérez, Emilio Itarte

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23 Citations (Scopus)


Casein kinase 2 was able to phosphorylate the β-subunit of hepatic insulin receptor in the presence of either ATP or GTP. Phosphorylation by casein kinase 2 was observed even in the absence of insulin, was inhibited by low heparin concentrations, and led to the incorporation of phosphate on serine and threonine residues. Casein kinase 2 phosphorylation of insulin receptor partially decreased its tyrosine kinase activity. © 1988.
Original languageEnglish
Pages (from-to)130-134
JournalFEBS Letters
Issue number1
Publication statusPublished - 9 May 1988


  • (Rat liver)
  • Casein kinase 2
  • Insulin receptor
  • Serine phosphorylation
  • Threonine phosphorylation


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