Please use this identifier to cite or link to this item: https://doi.org/10.1038/srep18773
Title: NuSAP modulates the dynamics of kinetochore microtubules by attenuating MCAK depolymerisation activity
Authors: Li, C 
Zhang, Y 
Yang, Q 
Ye, F 
Sun, S.Y
Chen, E.S 
Liou, Y.-C 
Keywords: AURKB protein, human
aurora B kinase
KIF2C protein, human
kinesin
microtubule associated protein
NuSAP protein, human
protein binding
cell line
centromere
human
metabolism
metaphase
microtubule
protein multimerization
protein stability
Aurora Kinase B
Cell Line
Humans
Kinesin
Kinetochores
Metaphase
Microtubule-Associated Proteins
Microtubules
Protein Binding
Protein Multimerization
Protein Stability
Issue Date: 2016
Publisher: Nature Publishing Group
Citation: Li, C, Zhang, Y, Yang, Q, Ye, F, Sun, S.Y, Chen, E.S, Liou, Y.-C (2016). NuSAP modulates the dynamics of kinetochore microtubules by attenuating MCAK depolymerisation activity. Scientific Reports 6 : 18773. ScholarBank@NUS Repository. https://doi.org/10.1038/srep18773
Abstract: Nucleolar and spindle-associated protein (NuSAP) is a microtubule-associated protein that functions as a microtubule stabiliser. Depletion of NuSAP leads to severe mitotic defects, however the mechanism by which NuSAP regulates mitosis remains elusive. In this study, we identify the microtubule depolymeriser, mitotic centromere-associated kinesin (MCAK), as a novel binding partner of NuSAP. We show that NuSAP regulates the dynamics and depolymerisation activity of MCAK. Phosphorylation of MCAK by Aurora B kinase, a component of the chromosomal passenger complex, significantly enhances the interaction of NuSAP with MCAK and modulates the effects of NuSAP on the depolymerisation activity of MCAK. Our results reveal an underlying mechanism by which NuSAP controls kinetochore microtubule dynamics spatially and temporally by modulating the depolymerisation function of MCAK in an Aurora B kinase-dependent manner. Hence, this study provides new insights into the function of NuSAP in spindle formation during mitosis. © 2015, Nature Publishing Group. All rights reserved.
Source Title: Scientific Reports
URI: https://scholarbank.nus.edu.sg/handle/10635/175448
ISSN: 20452322
DOI: 10.1038/srep18773
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