Abstract
Accurate control of cytokinesis is critical for genomic stability to complete high-fidelity transmission of genetic material to the next generation. A number of proteins accumulate in the intercellular bridge (midbody) during cytokinesis, and the dynamics of these proteins are temporally and spatially orchestrated to complete the process. In this study, we demonstrated that localization of centromere-associated protein-E (CENP-E) at the midbody is involved in cytokinetic abscission. The motor activity of CENP-E and the C-terminal midbody localization domain, which includes amino acids 2659–2666 (RYFDNSSL), are involved in the anchoring of CENP-E to the center of the midbody. Furthermore, CENP-E motor activity contributes to the accumulation of protein regulator of cytokinesis 1 (PRC1) in the midbody during cytokinesis. Midbody localization of PRC1 is critical to the antiparallel microtubule structure and recruitment of other midbody-associated proteins. Therefore, CENP-E motor activity appears to play important roles in the organization of these proteins to complete cytokinetic abscission. Our findings will be helpful for understanding how each step of cytokinesis is regulated to complete cytokinetic abscission.
Highlights
Cytokinesis, the final stage of cell division, distributes the replicated genome and other cellular components of the parent cell to the two daughter cells
Timelapse microscopy revealed that the duration of cytokinesis was significantly prolonged in siCENP-E + siBubR1 cells compared to siBubR1 and non-silencing control small interfering RNAs (siRNAs) cells
We investigated the molecular function of centromere-associated protein-E (CENP-E) at the midbody during cytokinetic abscission
Summary
Cytokinesis, the final stage of cell division, distributes the replicated genome and other cellular components of the parent cell to the two daughter cells. Following chromosome segregation at anaphase, a cytokinetic cleavage furrow divides the two nascent daughter cells. These post-mitotic daughter cells, remain connected by an intercellular bridge containing antiparallel arrays of microtubules that overlap at a central region termed the midbody until cytokinetic abscission splits these cells apart. The kinesin motor protein KIF4, which localizes at the midbody in a PRC1-dependent www.impactjournals.com/oncotarget manner, plays an important role in determining the size of antiparallel microtubule overlap at the anaphase central spindle. Signaling networks localized to the midbody via motor proteins appear critical for the organization and stabilization of a narrow zone of plus end overlap at the center of the midzone
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