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.
Ludwig Institute for Cancer Research, Biomedical Center, Uppsala, Sweden.
H
H
Ichijo
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H
Yamashita
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ten Dijke
Y
Y
Eto
C H
CH
Heldin
K
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Miyazono
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