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TRIP13 and APC15 drive mitotic exit by turnover of interphase- and unattached kinetochore-produced MCC

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Title
TRIP13 and APC15 drive mitotic exit by turnover of interphase- and unattached kinetochore-produced MCC
Author(s)
Dong Hyun Kim; Joo Seok Han; Peter Ly; Qiaozhen Ye; Moria A. McMahon; Kyungjae Myung; Kevin D. Corbett; Don W. Cleveland
Publication Date
2018-10
Journal
NATURE COMMUNICATIONS, v.9, no.1, pp.4354 -
Publisher
NATURE PUBLISHING GROUP
Abstract
The mitotic checkpoint ensures accurate chromosome segregation through assembly of the mitotic checkpoint complex (MCC), a soluble inhibitor of the anaphase-promoting complex/cyclosome (APC/C) produced by unattached kinetochores. MCC is also assembled during interphase by Mad1/Mad2 bound at nuclear pores, thereby preventing premature mitotic exit prior to kinetochore maturation and checkpoint activation. Using degron tagging to rapidly deplete the AAA+ ATPase TRIP13, we show that its catalytic activity is required to maintain a pool of open-state Mad2 for MCC assembly, thereby supporting mitotic checkpoint activation, but is also required for timely mitotic exit through catalytic disassembly of MCC. Strikingly, combining TRIP13 depletion with elimination of APC15-dependent Cdc20 ubiquitination/degradation results in a complete inability to exit mitosis, even when MCC assembly at unattached kinetochores is prevented. Thus, mitotic exit requires MCC produced either in interphase or mitosis to be disassembled by TRIP13-catalyzed removal of Mad2 or APC15-driven ubiquitination/degradation of its Cdc20 subunit. © The Author(s) 2018
URI
https://pr.ibs.re.kr/handle/8788114/5108
ISSN
2041-1723
Appears in Collections:
Center for Genomic Integrity(유전체 항상성 연구단) > Journal Papers (저널논문)
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