Mps1激酶催化活性的失活阻止了其在中心体上的降解。

Shrabani Halder, Arpita Dutta, Rupsa Mondal, Banhi Chowdhury, Benu Brata Das, Shubhra Majumder
{"title":"Mps1激酶催化活性的失活阻止了其在中心体上的降解。","authors":"Shrabani Halder, Arpita Dutta, Rupsa Mondal, Banhi Chowdhury, Benu Brata Das, Shubhra Majumder","doi":"10.1002/cm.22032","DOIUrl":null,"url":null,"abstract":"<p><p>Mps1 kinase plays important roles in regulating centriole assembly, apart from its essential role in spindle assembly checkpoint. Here we report a novel mode of regulating centrosomal Mps1 level, which is governed by its own catalytic activity that promotes its degradation at centrosomes. A kinase-dead mutant of Mps1 or catalytically inactive Mps1 due to treatment with a specific kinase inhibitor is protected from degradation at centrosomes. This autoregulatory mode of controlling Mps1 activity at centrosomes likely restricts excess centriole production in a dividing cell.</p>","PeriodicalId":72766,"journal":{"name":"Cytoskeleton (Hoboken, N.J.)","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-04-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Inactivation of the Catalytic Activity of Mps1 Kinase Prevents Its Own Degradation at Centrosomes.\",\"authors\":\"Shrabani Halder, Arpita Dutta, Rupsa Mondal, Banhi Chowdhury, Benu Brata Das, Shubhra Majumder\",\"doi\":\"10.1002/cm.22032\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Mps1 kinase plays important roles in regulating centriole assembly, apart from its essential role in spindle assembly checkpoint. Here we report a novel mode of regulating centrosomal Mps1 level, which is governed by its own catalytic activity that promotes its degradation at centrosomes. A kinase-dead mutant of Mps1 or catalytically inactive Mps1 due to treatment with a specific kinase inhibitor is protected from degradation at centrosomes. This autoregulatory mode of controlling Mps1 activity at centrosomes likely restricts excess centriole production in a dividing cell.</p>\",\"PeriodicalId\":72766,\"journal\":{\"name\":\"Cytoskeleton (Hoboken, N.J.)\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-04-21\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cytoskeleton (Hoboken, N.J.)\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/cm.22032\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cytoskeleton (Hoboken, N.J.)","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/cm.22032","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

摘要

Mps1激酶除了在纺锤体组装检查点中发挥重要作用外,在中心粒组装中也起着重要的调节作用。在这里,我们报告了一种调节中心体Mps1水平的新模式,该模式由其自身的催化活性控制,促进其在中心体上的降解。激酶死亡突变的Mps1或催化失活的Mps1由于特定的激酶抑制剂处理,在中心体上被保护免受降解。这种控制中心体上Mps1活性的自动调节模式可能限制了分裂细胞中过多的中心粒产生。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Inactivation of the Catalytic Activity of Mps1 Kinase Prevents Its Own Degradation at Centrosomes.

Mps1 kinase plays important roles in regulating centriole assembly, apart from its essential role in spindle assembly checkpoint. Here we report a novel mode of regulating centrosomal Mps1 level, which is governed by its own catalytic activity that promotes its degradation at centrosomes. A kinase-dead mutant of Mps1 or catalytically inactive Mps1 due to treatment with a specific kinase inhibitor is protected from degradation at centrosomes. This autoregulatory mode of controlling Mps1 activity at centrosomes likely restricts excess centriole production in a dividing cell.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信