| First Author | Zhu X | Year | 1995 |
| Journal | J Biol Chem | Volume | 270 |
| Issue | 33 | Pages | 19545-50 |
| PubMed ID | 7642639 | Mgi Jnum | J:124853 |
| Mgi Id | MGI:3722702 | Doi | 10.1074/jbc.270.33.19545 |
| Citation | Zhu X, et al. (1995) The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization. J Biol Chem 270(33):19545-50 |
| abstractText | Mitosin is a novel 350-kDa nuclear phosphoprotein that dramatically relocates from the evenly nuclear distribution in S phase to the centromere/kinetochore and mitotic apparatus in M phase. The dynamic relocalization of mitosin is accompanied by the phosphorylation of itself, suggesting that mitosin plays a role in mitotic progression. The molecular basis of nuclear localization and targeting of mitosin to the centromere/kinetochore were characterized using a set of epitope-tagged deletion mutants. The data indicate that the extreme C terminus (amino acids 2,487-3,113) of mitosin has both an independent centromere/kinetochore targeting domain and an unusually spaced bipartite nuclear localization signal. Moreover, the same centromere/kinetochore targeting domain was shown to be essential for the ability of mitosin to bind to itself or other putative mitosin-associated proteins through use of the yeast two-hybrid system. These results suggest that the C terminus of the mitosin is essential for its role in influencing cell cycle progression. |
