| First Author | Aurisicchio L | Year | 1998 |
| Journal | J Biol Chem | Volume | 273 |
| Issue | 3 | Pages | 1477-82 |
| PubMed ID | 9430685 | Mgi Jnum | J:45295 |
| Mgi Id | MGI:1194981 | Doi | 10.1074/jbc.273.3.1477 |
| Citation | Aurisicchio L, et al. (1998) Identification of the thyroid transcription factor-1 as a target for rat MST2 kinase. J Biol Chem 273(3):1477-82 |
| abstractText | Thyroid transcription factor-1 (TTF-1) is a homeodomain-containing transcription factor that is required for thyroid-specific expression of the thyroglobulin and thyroperoxidase genes as well as for lung-specific expression of the surfactant protein A, B, and C and the CC10 and the HNF-3 alpha genes. TTF-1 is a phosphoprotein, and the phosphorylation of TTF-1 has been studied already. However, the kinase(s) that could be responsible for this phosphorylation have not been known. In this paper we report the identification by in-gel kinase assay of a 56-kDa serine/threonine kinase that is able to phosphorylate TTF-1 in thyroid cells. The cloning of this kinase revealed that we had identified the rat homolog of the human MST2 kinase. The pathway in which human MST2 functions is not known; however, it does not appear to involve either mitogen-activated protein kinases such as Erk1 and Erk2 nor the stress-activated protein kinases such as JNK and p38. We show that the activity responsible for TTF-1 phosphorylation is constitutive in thyroid cells. Furthermore, we demonstrate that TTF-1 is phosphorylated in vivo by rMST2 at the same residues that had been identified previously as the major phosphorylation sites. Thus, TTF-1 represents the first identified target of this class of protein kinases. |
