| First Author | Maita H | Year | 2000 |
| Journal | Eur J Biochem | Volume | 267 |
| Issue | 16 | Pages | 5168-78 |
| PubMed ID | 10931201 | Mgi Jnum | J:63919 |
| Mgi Id | MGI:1888410 | Doi | 10.1046/j.1432-1327.2000.01585.x |
| Citation | Maita H, et al. (2000) PAP-1, a novel target protein of phosphorylation by pim-1 kinase. Eur J Biochem 267(16):5168-78 |
| abstractText | Protooncogene, pim-1, has been reported to be a predisposition for lymphomagenesis along with myc, and its protein product, Pim-1, has been shown to be a serine/threonine protein kinase, whose activity is involved in proliferation and differentiation of blood cells. The signal transduction pathways neither to nor from Pim-1, however, have been clarified. We have cloned a cDNA encoding a novel Pim-1 binding protein, PAP-1, comprising 213 amino acids with a basic amino-acid cluster near the C-terminus. PAP-1 was colocalized with Pim-1 in human HeLa cell nuclei. The in vitro binding assays using GST fusion proteins of the wild-type and various deletion mutants revealed that the whole molecule of Pim-1 is required for the binding activity to PAP-1 and that Pim-1 binds to the region from amino-acid numbers 1-147 of PAP-1, or to two segments in the region. The association of PAP-1 with Pim-1 was also shown in vivo in transfected cells. Furthermore, PAP-1 was phosphorylated in vitro by Pim-1, but not a kinase-negative Pim-1 mutant. The two serine residues of PAP-1 at amino acids 204 and 206 near the C-terminus were phosphorylated by Pim-1. PAP-1 is thus thought to be a target protein for Pim-1 kinase. |
