Abstract
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 language | English |
---|---|
Pages (from-to) | 21-24 |
Journal | FEBS Letters |
Volume | 264 |
Issue number | 1 |
DOIs | |
Publication status | Published - 7 May 1990 |
Keywords
- Casein kinase-1
- Phosphotyrosine
- Protein
- Protein kinase