{"title":"接触和交流:ZO-2和河马通路。","authors":"Miranda Thomas","doi":"10.1111/febs.17417","DOIUrl":null,"url":null,"abstract":"<p>The PDZ domain-containing protein ZO-2 is defined as a tight junction (TJ) protein, but is also known to have a role in the maintenance of cellular apicobasal polarity and to function as a signalling molecule in several pathways, including the Hippo pathway. In this issue, Liu OX <i>et al.</i> [(2024) <i>FEBS J</i>, https://doi.org/10.1111/febs.17304] report how the multiple protein binding sites of ZO2 protein allow it to act as a scaffold to facilitate its signalling functions.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":"292 7","pages":"1584-1586"},"PeriodicalIF":0.0000,"publicationDate":"2025-02-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1111/febs.17417","citationCount":"0","resultStr":"{\"title\":\"Contact and communication: ZO-2 and the Hippo pathway\",\"authors\":\"Miranda Thomas\",\"doi\":\"10.1111/febs.17417\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>The PDZ domain-containing protein ZO-2 is defined as a tight junction (TJ) protein, but is also known to have a role in the maintenance of cellular apicobasal polarity and to function as a signalling molecule in several pathways, including the Hippo pathway. In this issue, Liu OX <i>et al.</i> [(2024) <i>FEBS J</i>, https://doi.org/10.1111/febs.17304] report how the multiple protein binding sites of ZO2 protein allow it to act as a scaffold to facilitate its signalling functions.</p>\",\"PeriodicalId\":94226,\"journal\":{\"name\":\"The FEBS journal\",\"volume\":\"292 7\",\"pages\":\"1584-1586\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-02-05\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://onlinelibrary.wiley.com/doi/epdf/10.1111/febs.17417\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The FEBS journal\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1111/febs.17417\",\"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 FEBS journal","FirstCategoryId":"1085","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1111/febs.17417","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Contact and communication: ZO-2 and the Hippo pathway
The PDZ domain-containing protein ZO-2 is defined as a tight junction (TJ) protein, but is also known to have a role in the maintenance of cellular apicobasal polarity and to function as a signalling molecule in several pathways, including the Hippo pathway. In this issue, Liu OX et al. [(2024) FEBS J, https://doi.org/10.1111/febs.17304] report how the multiple protein binding sites of ZO2 protein allow it to act as a scaffold to facilitate its signalling functions.