A tripartite mechanism catalyzes Mad2-Cdc20 assembly at unattached kinetochores.
A tripartite mechanism catalyzes Mad2-Cdc20 assembly at unattached kinetochores.
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DOI：
10.1126/science.abc1424
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发表时间：
2021-01-01
期刊：
影响因子：
--
通讯作者：
Desai A
中科院分区：
文献类型：
--
作者：
Lara-Gonzalez P;Kim T;Oegema K;Corbett K;Desai A
During cell division, kinetochores couple chromosomes to spindle microtubules. To protect against chromosome gain or loss, kinetochores lacking microtubule attachment locally catalyze association of the checkpoint proteins Cdc20 and Mad2, which is the key event in the formation of a diffusible checkpoint complex that prevents mitotic exit. We elucidated the mechanism of kinetochore-catalyzed Mad2–Cdc20 assembly with a probe that specifically monitors this assembly reaction at kinetochores in living cells. Catalysis occurred through a tripartite mechanism that included localized delivery of Mad2 and Cdc20 substrates and two phospho-dependent interactions that geometrically constrained their positions and primed Cdc20 for interaction with Mad2. These results reveal how unattached kinetochores create a signal that ensures genome integrity during cell division. A tripartite mechanism explains how the kinetic barrier to mitotic checkpoint complex assembly is overcome at kinetochores.
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影响因子：
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