Arabidopsis KNL1 recruits type one protein phosphatase to kinetochores to silence the spindle assembly checkpoint

IF 12.5 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES Science Advances Pub Date : 2025-02-05 DOI:10.1126/sciadv.adq4033
Ying He, Xiaoya Tang, Hao Fu, Yihang Tang, Honghui Lin, Xingguang Deng
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Abstract

Proper chromosome segregation during cell division is essential for genomic integrity and organismal development. This process is monitored by the spindle assembly checkpoint (SAC), which delays anaphase onset until all chromosomes are properly attached to the mitotic spindle. The kinetochore protein KNL1 plays a critical role in recruiting SAC proteins. Here, we reveal that Arabidopsis KNL1 regulates SAC silencing through the direct recruitment of type one protein phosphatase (TOPP) to kinetochores. We show that KNL1 interacts with all nine TOPPs via a conserved RVSF motif in its N terminus, and this interaction is required for the proper localization of TOPPs to kinetochores during mitosis. Disrupting KNL1-TOPP interaction leads to persistent SAC activation, resulting in a severe metaphase arrest and defects in plant growth and development. Our findings highlight the evolutionary conservation of KNL1 in coordinating kinetochore-localized phosphatase to ensure timely SAC silencing and faithful chromosome segregation in Arabidopsis .
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拟南芥KNL1招募1型蛋白磷酸酶到着丝点以沉默纺锤体组装检查点
细胞分裂过程中正确的染色体分离对基因组完整性和生物体发育至关重要。这个过程由纺锤体组装检查点(SAC)监控,它延迟后期开始,直到所有染色体都正确地附着在有丝分裂纺锤体上。着丝点蛋白KNL1在募集SAC蛋白中起关键作用。在这里,我们揭示了拟南芥KNL1通过直接募集1型蛋白磷酸酶(TOPP)到着丝点来调节SAC沉默。我们发现KNL1通过其N端保守的RVSF基序与所有9个topp相互作用,并且这种相互作用是有丝分裂期间topp正确定位到着丝点所必需的。破坏KNL1-TOPP相互作用会导致SAC持续激活,导致严重的中期阻滞和植物生长发育缺陷。我们的研究结果强调了KNL1在拟南芥中协调着丝点定位磷酸酶以确保及时的SAC沉默和忠实的染色体分离的进化保守性。
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来源期刊
Science Advances
Science Advances 综合性期刊-综合性期刊
CiteScore
21.40
自引率
1.50%
发文量
1937
审稿时长
29 weeks
期刊介绍: Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.
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