{"title":"Protein kinase A: a quirky prototype.","authors":"Matthew G Gold","doi":"10.1111/febs.70176","DOIUrl":null,"url":null,"abstract":"<p><p>Protein kinase A (PKA) has served as a prototype for establishing kinase fundamentals, including sequence, structure and catalytic mechanism. However, PKA is quirky in some respects. Its regulatory elements are expressed separately, including type I (RI) regulatory subunits that contain unusual disulphide-linked dimerization and docking domains. Benjamin-Zukerman and colleagues report on the RIβ mutation L50R that disrupts this domain to cause neuronal loss and parkinsonism driven by a PKA mutation. They show that PKA catalytic subunits are released more easily from RIβ subunits containing the L50R mutation, adding depth to our understanding of this neurodevelopmental disorder.</p>","PeriodicalId":94226,"journal":{"name":"The FEBS journal","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-07-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"The FEBS journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1111/febs.70176","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Protein kinase A (PKA) has served as a prototype for establishing kinase fundamentals, including sequence, structure and catalytic mechanism. However, PKA is quirky in some respects. Its regulatory elements are expressed separately, including type I (RI) regulatory subunits that contain unusual disulphide-linked dimerization and docking domains. Benjamin-Zukerman and colleagues report on the RIβ mutation L50R that disrupts this domain to cause neuronal loss and parkinsonism driven by a PKA mutation. They show that PKA catalytic subunits are released more easily from RIβ subunits containing the L50R mutation, adding depth to our understanding of this neurodevelopmental disorder.