Phosphorylation of smg p21B/rap1B p21 by cyclic GMP-dependent protein kinase.
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.
Miura
Y
Y
Department of Biochemistry, Kobe University School of Medicine, Japan.
Kaibuchi
K
K
Itoh
T
T
Corbin
J D
JD
Francis
S H
SH
Takai
Y
Y
D001345:Autoradiography; D002474:Cell-Free System; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D019204:GTP-Binding Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011518:Proto-Oncogene Proteins / Q000378:metabolism*; D020668:rap GTP-Binding Proteins
D011518:Proto-Oncogene Proteins; D011494:Protein Kinases; D019204:GTP-Binding Proteins; D020668:rap GTP-Binding Proteins