Fol. Biol. 2013, 59, 105-109
Transfer of Ser7 Phosphorylated CENP-A from Centromere to Midbody During Mitosis in MCF-7 Cells
Serine 7 of centromere protein A (CENP-A) is a very important mitosis-specific phosphorylation site. In this study, we demonstrate the subcellular distribution of Ser7 phosphorylated CENP-A during mitosis in MCF-7 cells. The Ser7 phosphorylation of CENP-A was observed beginning at prophase at centromeres. Upon progression of mitosis, the fluorescence signals emerged in the central region of the metaphase plate and were maintained until anaphase at centromeres. At late anaphase, the fluorescence signals moved to the midzone gradually and transferred from the centromere to the midbody completely at telophase. They were compacted into the centre of the midbody in a thin cylinder consisting of a sandglass-like “mitotic machine” with microtubules and condensed chromosome. We also found that Ser10 phosphorylated H3 and Thr11 phosphorylated H3 were co-localized at the midbody in two bell-like symmetrical bodies with Ser7 phosphorylated CENP-A during the terminal stage of cytokinesis. Midbody isolation and immunoblotting experiments also indicated that Ser7 phosphorylated CENP-A are components of the midbody. These findings suggest that Ser7 phosphorylated CENP-A acts as a chromosomal passenger protein and may play an important role in cytokinesis.
Keywords
Ser7 phosphorylated CENP-A, centromere, midbody, cytokinesis.
Funding
This work was partially supported by the Fundamental Research Funds for the Central Universities (65011621) and National Natural Science Foundation of China (31100527).
References
Copyright
This is an open-access article distributed under the terms of the Creative Commons Attribution License.
