| First Author | Nakamura T | Year | 1992 |
| Journal | J Biol Chem | Volume | 267 |
| Issue | 26 | Pages | 18924-8 |
| PubMed ID | 1326537 | Mgi Jnum | J:2521 |
| Mgi Id | MGI:51043 | Doi | 10.1016/s0021-9258(19)37049-8 |
| Citation | Nakamura T, et al. (1992) Isolation and characterization of activin receptor from mouse embryonal carcinoma cells. Identification of its serine/threonine/tyrosine protein kinase activity. J Biol Chem 267(26):18924-8 |
| abstractText | The activin receptor protein was isolated from the mouse embryonal carcinoma (EC) cell line P19 by three cycles of affinity chromatography on an activin A-immobilized column. The purified receptor had a specific and high affinity for activins A, AB, and B (Kd = 345 pM), but not for transforming growth factor beta. The purified activin receptor was identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and ligand blotting analysis as a single protein of 70 kDa. The amino acid sequence of the first 18 NH2-terminal residues revealed that the receptor is a member of the activin receptor family. The purified receptor phosphorylated itself and exogenous substrate proteins on serine, threonine, and tyrosine residues, indicating that the activin receptor is a transmembrane serine/threonine/tyrosine protein kinase. These results suggest that signal transduction of activin employs a novel pathway via a new class of cellular receptor in EC P19 cells. |
