Citron kinase interacts with LATS2 and inhibits its activity by occluding its hydrophobic phosphorylation motif
作者机构：Department of Biological SciencesKAIST 291 Daehak-roYuseong-guDaejeon 34141Republic of Korea Department of Molecular Biotechnology and Health SciencesUniversity of Turin10126 TurinItaly
出 版 物：《Journal of Molecular Cell Biology》 (分子细胞生物学报（英文版）)
年 卷 期：2019年第11卷第11期
页 面：1006-1017页
核心收录：
学科分类：1002[医学-临床医学] 100214[医学-肿瘤学] 10[医学]
基 金：supported by grants from National Creative Research Initiative Program Individual Basic Science & Engineering Research Program Global Research Laboratory Program Mid-Career Research Program Ministry of Education of the Republic of Korea and the National Research Foundation of Korea Korean Advanced Institute of Science and Technology
主 题：citron kinase LATS2-YAP interaction LATS2 inhibition sticky-warts Hippo pathway
摘 要：The inhibitory effect of large tumor suppressor kinase(LATS1/2)on the activity of the oncoprotein yes-associated protein(YAP)is crucial to maintain tissue *** studies have identified several new regulators of this ***,citron kinase(CIT)was listed as a potential binding candidate of Hippo-related components,suggesting a new connection between CIT and the Hippo *** from CITs role in cytokinesis,the molecular crosstalk between CIT and the Hippo pathway is largely ***,we demonstrate a role for CIT as a scaffold protein Unking LATS2 and *** importantly,CIT interacts with LATS2 to directly suppress LATS2 phosphorylation at the hydrophobic motif—targeted by MST1,leading to LATS2 inactivation and YAP *** studying their genetic interactions,we found that Sticky,the CIT homolog in Drosophila melanogaster,functions with Warts to control Drosophila eye ***,our study confirms citron kinase as a novel regulator of the Hippo pathway.
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