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PMID:27030108
| Citation |
Iimori, M, Watanabe, S, Kiyonari, S, Matsuoka, K, Sakasai, R, Saeki, H, Oki, E, Kitao, H and Maehara, Y (2016) Phosphorylation of EB2 by Aurora B and CDK1 ensures mitotic progression and genome stability. Nat Commun 7:11117 |
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| Abstract |
Temporal regulation of microtubule dynamics is essential for proper progression of mitosis and control of microtubule plus-end tracking proteins by phosphorylation is an essential component of this regulation. Here we show that Aurora B and CDK1 phosphorylate microtubule end-binding protein 2 (EB2) at multiple sites within the amino terminus and a cluster of serine/threonine residues in the linker connecting the calponin homology and end-binding homology domains. EB2 phosphorylation, which is strictly associated with mitotic entry and progression, reduces the binding affinity of EB2 for microtubules. Expression of non-phosphorylatable EB2 induces stable kinetochore microtubule dynamics and delays formation of bipolar metaphase plates in a microtubule binding-dependent manner, and leads to aneuploidy even in unperturbed mitosis. We propose that Aurora B and CDK1 temporally regulate the binding affinity of EB2 for microtubules, thereby ensuring kinetochore microtubule dynamics, proper mitotic progression and genome stability. |
| Links |
PubMed Online version:10.1038/ncomms11117 |
| Keywords |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0004674: protein serine/threonine kinase activity |
ECO:0000314: |
F |
Figure 4 |
complete | ||||
Notes
See also
References
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