The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo

Mol Cell Biol. 1986 Jul;6(7):2738-44. doi: 10.1128/mcb.6.7.2738-2744.1986.

Abstract

p36, a major in vivo substrate of protein-tyrosine kinases, is shown to be phosphorylated at serine 25, a site very close to the major site of tyrosine phosphorylation by pp60v-src, tyrosine 23 (J. R. Glenney, Jr., and B. F. Tack, Proc. Natl. Acad. Sci. USA 82:7884-7888, 1985). We present evidence suggesting that protein kinase C mediates phosphorylation of serine 25.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Annexins
  • Cattle
  • Membrane Proteins / metabolism*
  • Phosphoproteins / analysis
  • Protein Kinase C / metabolism*
  • Protein-Tyrosine Kinases / metabolism*
  • Substrate Specificity

Substances

  • Annexins
  • Membrane Proteins
  • Phosphoproteins
  • Protein-Tyrosine Kinases
  • Protein Kinase C