Abstract
The inhibitor of apoptosis protein survivin is implicated in two key
biological events: in the control of cell proliferation and in the
regulation of cell lifespan. Although the details of mitotic roles of
survivin are unclear, the protein appears to modulate microtubule
function and might participate in regulating the spindle checkpoint.
Survivin physically associates with Aurora B, a serine-threonine kinase
involved in microtubule attachment to centromeres and regulation of
chromosome segregation. Here we have examined the dynamics and
localization of a survivin-GFP chimera using high-resolution
fluorescence microscopy and photobleaching. Survivin forms a bi-partite
structure at the inner centromere that undergoes significant stretching
during mitosis. Photobleaching experiments revealed marked changes in
rates of survivin turnover at centromeres. These were regulated by stage
of the cell cycle, microtubule attachment, and Aurora B kinase
activity. We hypothesize that changes in the turnover of survivin at
centromeres influence the stability of kinetochore-microtubule
attachment and signaling of the spindle checkpoint.
Original language | English |
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Pages (from-to) | 4033-4042 |
Journal | Journal of Cell Science |
Volume | 117 |
DOIs | |
Publication status | Published - 2004 |
MoE publication type | A1 Journal article-refereed |
Keywords
- Survivin
- Microtubules
- Mitosis
- Spindle checkpoint
- FRAP