Characterization of in vivo phosphorylation of activin type II receptor.
An antiserum was generated against a C-terminal peptide of the mouse activin type II receptor (ActR-II), which specifically immunoprecipitates ActR-II protein transiently expressed in COS-1 cells. Autophosphorylation activity of the ActR-II was examined in [32P]orthophosphate labeled COS-1 cells. The immunoprecipitated ActR-II protein was found to be phosphorylated on serine residues in the absence of ligand stimulation, and the phosphorylation was slightly increased after stimulation with activin A.
Ichijo
H
H
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
Yamashita
H
H
ten Dijke
P
P
Eto
Y
Y
Heldin
C H
CH
Miyazono
K
K
D029404:Activin Receptors; D028341:Activins; D000595:Amino Acid Sequence; D000818:Animals; D002478:Cells, Cultured; D007265:Inhibins / Q000378:metabolism*; D051379:Mice; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000276:immunology; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000276:immunology / Q000378:metabolism*; D011956:Receptors, Cell Surface / Q000276:immunology / Q000378:metabolism*; D013379:Substrate Specificity; D014162:Transfection
D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D028341:Activins; D007265:Inhibins; D017346:Protein Serine-Threonine Kinases; D029404:Activin Receptors