Phosphorylation and activation of p40 tyrosine kinase by casein kinase-1

Jordi Vila, D. Michael Payne, Thomas F. Zioncheck, Marietta L. Harrison, Emilio Itarte, Michael J. Weber

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)


Because examination of regulatory trans-phosphorylations can help elucidate the cellular functions of tyrosyi protein kinases, we have investigated the effects of phosphorylation by casein kinase-1 on the activity of the p40 tyrosyi protein kinase. We find that casein kinase-1 can phosphorylate the p40 tyrosyl kinase on serine and threonine residues, in part on a unique tryptic peptide. The phosphorylation induces a substantial increase in the tyrosyl protein kinase activity of p40, in contrast to most instances in which serine/threonine phosphorylation inhibits activity of tyrosyl protein kinases. These findings raise the possibility that p40 might be part of a protein phosphorylation network in which casein kinase-1 participates. © 1990.
Original languageEnglish
Pages (from-to)21-24
JournalFEBS Letters
Issue number1
Publication statusPublished - 7 May 1990


  • Casein kinase-1
  • Phosphotyrosine
  • Protein
  • Protein kinase


Dive into the research topics of 'Phosphorylation and activation of p40 tyrosine kinase by casein kinase-1'. Together they form a unique fingerprint.

Cite this