Abelson murine leukaemia virus protein is phosphorylated in vitro to form phosphotyrosine

Nature. 1980 Feb 28;283(5750):826-31. doi: 10.1038/283826a0.

Abstract

The Abelson murine leukaemia virus protein (P120) can become phosphorylated in vitro by [gamma-32P]ATP. The protein has been purified from cell membranes to the point that in specific conditions virtually all of the incorporated 32P is in P120. The reaction is stimulated by Mn2+ and Mg2+ but not Ca2+ and is very rapid even at 0 degrees C. The phosphate is linked to P120 at tyrosine, a linkage not previously reported for a phosphorylation reaction. Phosphorylation may be involved in the transforming activity of viruses that cause leukaemia as well as sarcomas.

Publication types

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

MeSH terms

  • Abelson murine leukemia virus / metabolism*
  • Animals
  • Antigens, Neoplasm
  • Antigens, Viral
  • Avian Sarcoma Viruses / metabolism
  • Cell Transformation, Viral*
  • Kinetics
  • Leukemia Virus, Murine / metabolism*
  • Membrane Proteins / metabolism
  • Mice
  • Phosphorylation
  • Protein Kinases / metabolism
  • Sarcoma, Experimental / metabolism
  • Tyrosine / analogs & derivatives
  • Viral Proteins / metabolism*

Substances

  • Antigens, Neoplasm
  • Antigens, Viral
  • Membrane Proteins
  • Viral Proteins
  • Tyrosine
  • Protein Kinases