P. Atherton, Franziska Lausecker, Alexandre F. Carisey, A. Gilmore, D. Critchley, I. Barsukov, C. Ballestrem
{"title":"talin自身抑制的解除触发了与血管蛋白的力无关的关联","authors":"P. Atherton, Franziska Lausecker, Alexandre F. Carisey, A. Gilmore, D. Critchley, I. Barsukov, C. Ballestrem","doi":"10.1083/jcb.201903134","DOIUrl":null,"url":null,"abstract":"Talin and vinculin control mechanosensing by linking adhesion receptors to the contractile actin cytoskeleton. Using a mitochondrial targeting system, Atherton et al. elucidate mechanisms regulating conformational changes required for vinculin binding to talin. Such activation mechanisms are not required for either protein to interact with the adhesion regulatory protein paxillin.","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":"49 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2019-12-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"40","resultStr":"{\"title\":\"Relief of talin autoinhibition triggers a force-independent association with vinculin\",\"authors\":\"P. Atherton, Franziska Lausecker, Alexandre F. Carisey, A. Gilmore, D. Critchley, I. Barsukov, C. Ballestrem\",\"doi\":\"10.1083/jcb.201903134\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Talin and vinculin control mechanosensing by linking adhesion receptors to the contractile actin cytoskeleton. Using a mitochondrial targeting system, Atherton et al. elucidate mechanisms regulating conformational changes required for vinculin binding to talin. Such activation mechanisms are not required for either protein to interact with the adhesion regulatory protein paxillin.\",\"PeriodicalId\":343306,\"journal\":{\"name\":\"The Journal of Cell Biology\",\"volume\":\"49 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-12-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"40\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Journal of Cell Biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1083/jcb.201903134\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Cell Biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1083/jcb.201903134","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Relief of talin autoinhibition triggers a force-independent association with vinculin
Talin and vinculin control mechanosensing by linking adhesion receptors to the contractile actin cytoskeleton. Using a mitochondrial targeting system, Atherton et al. elucidate mechanisms regulating conformational changes required for vinculin binding to talin. Such activation mechanisms are not required for either protein to interact with the adhesion regulatory protein paxillin.