Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase

FEBS Lett. 1992 Feb 3;297(1-2):171-4. doi: 10.1016/0014-5793(92)80353-i.

Abstract

smg p21B/rap1B p21, a member of ras p21-like small GTP-binding protein superfamily, has been shown to be phosphorylated by cyclic AMP-dependent protein kinase (protein kinase A). We show here that this protein was also phosphorylated by cyclic GMP-dependent protein kinase (protein kinase G) in a cell-free system. The same serine residue (Ser179) in the C-terminal region was phosphorylated by both protein kinases G and A. The Km and Vmax values of smg p21B for protein kinase G were 5 x 10(-7) M and 4 x 10(-9) mol/min/mg, and those values for protein kinase A were 1 x 10(-7) M and 3 x 10(-8) mol/min/mg.

Publication types

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

MeSH terms

  • Autoradiography
  • Cell-Free System
  • Chromatography, Liquid
  • Electrophoresis, Polyacrylamide Gel
  • GTP-Binding Proteins / metabolism*
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Proto-Oncogene Proteins / metabolism*
  • rap GTP-Binding Proteins

Substances

  • Proto-Oncogene Proteins
  • Protein Kinases
  • GTP-Binding Proteins
  • rap GTP-Binding Proteins