期刊
FEBS LETTERS
卷 588, 期 17, 页码 3265-3273出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2014.07.011
关键词
Mitotic checkpoint; Checkpoint silencing: cytoplasmic dynein; Mad1; Mad2; Bub1; BubR1; Bub3; Hec1; Mis12
资金
- CESPU [02-GCQF-CICS-2011N]
- national Portuguese funding through FCT - Fundacao para a Ciencia e a Tecnologia FCT [POCTI/BIA/PRO/60337/2004, PTDC/SAU-OBD/105234/2008]
- FCT [PEst-OE/ EQB/LA0023/2013, SFRH/BD/90744/2012]
- [EXPL/BEX-BCM/1104/2013]
- Fundação para a Ciência e a Tecnologia [SFRH/BD/90744/2012, PEst-OE/EQB/LA0023/2013, PTDC/SAU-OBD/105234/2008, POCI/BIA-PRO/60337/2004, EXPL/BEX-BCM/1104/2013] Funding Source: FCT
A predominant mechanism of spindle assembly checkpoint (SAC) silencing is dynein-mediated transport of certain kinetochore proteins along microtubules. There are still conflicting data as to which SAC proteins are dynein cargoes. Using two ATP reduction assays, we found that the core SAC proteins Mad1, Mad2, Bub1, BubR1, and Bub3 redistributed from attached kinetochores to spindle poles, in a dynein-dependent manner. This redistribution still occurred in metaphase-arrested cells, at a time when the SAC should be satisfied and silenced. Unexpectedly, we found that a pool of Hec1 and Mis12 also relocalizes to spindle poles, suggesting KMN components as additional dynein cargoes. The potential significance of these results for SAC silencing is discussed. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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