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Subcellular Biochemistry 101 Adrienne L. Edkins Gregory L. Blatch Editors The Networking of Chaperones by Co-Chaperones Third Edition Subcellular Biochemistry Volume 101 SeriesEditor J. Robin Harris, Institute of Molecular Physiology, University of Mainz, Mainz, Germany AdvisoryEditors TapasK.Kundu,TranscriptionandDiseaseLaboratory,JNCASR,Bangalore,India ViktorKorolchuk,InstituteforCellandMolecularBiosciences,Newcastle University,NewcastleuponTyne,UK VictorBolanos-Garcia,DepartmentofBiologicalandMedicalSciences,Oxford BrookesUniversity,Oxford,UK JonMarles-Wright,SchoolofNaturalandEnvironmentalSciences,Newcastle University,NewcastleuponTyne,UK The book series SUBCELLULAR BIOCHEMISTRY is a renowned and well recognized forum for disseminating advances of emerging topics in Cell Biology and related subjects. All volumes are edited by established scientists and the individual chapters are written by experts on the relevant topic. The individual chaptersofeachvolumearefullycitableandindexedinMedline/Pubmedtoensure maximumvisibilityofthework. (cid:129) Adrienne L. Edkins Gregory L. Blatch Editors The Networking of Chaperones by Co-Chaperones Third Edition Editors AdrienneL.Edkins GregoryL.Blatch BiomedicalBiotechnologyResearchUnit, FacultyofHealthSciences DepartmentofBiochemistryand HigherCollegesofTechnology Microbiology Sharjah,UnitedArabEmirates RhodesUniversity Grahamstown,SouthAfrica ISSN0306-0225 ISSN2542-8810 (electronic) SubcellularBiochemistry ISBN978-3-031-14739-5 ISBN978-3-031-14740-1 (eBook) https://doi.org/10.1007/978-3-031-14740-1 ©TheEditor(s)(ifapplicable)andTheAuthor(s),underexclusivelicensetoSpringerNatureSwitzerland AG2007,2015,2023 Thisworkissubjecttocopyright.AllrightsaresolelyandexclusivelylicensedbythePublisher,whether thewholeorpartofthematerialisconcerned,specificallytherightsoftranslation,reprinting,reuseof illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similarordissimilarmethodologynowknownorhereafterdeveloped. Theuseofgeneraldescriptivenames,registerednames,trademarks,servicemarks,etc.inthispublication doesnotimply,evenintheabsenceofaspecificstatement,thatsuchnamesareexemptfromtherelevant protectivelawsandregulationsandthereforefreeforgeneraluse. The publisher, the authors, and the editorsare safeto assume that the adviceand informationin this bookarebelievedtobetrueandaccurateatthedateofpublication.Neitherthepublishernortheauthorsor theeditorsgiveawarranty,expressedorimplied,withrespecttothematerialcontainedhereinorforany errorsoromissionsthatmayhavebeenmade.Thepublisherremainsneutralwithregardtojurisdictional claimsinpublishedmapsandinstitutionalaffiliations. ThisSpringerimprintispublishedbytheregisteredcompanySpringerNatureSwitzerlandAG Theregisteredcompanyaddressis:Gewerbestrasse11,6330Cham,Switzerland Preface WeweresomewhatsurprisedwhenNatureSpringerinvitedustoconsiderproducing a third edition of our book The Networking of Chaperones by Co-chaperones. However, the downloads and citation data revealed that the second edition of the book(publishedin2015)hadbeenverywellreceivedbythescientificcommunity. Wewerepleasedtolearnthatallcontributedvolumespublishedin2015withinthe Nature Springer Biomedicine/Lifesciences portfolio (except handbooks and ency- clopaedias)accumulatedonaverageonlyhalfofthedownloadsincomparisontoour book. Based on the impressive performance of the book and given the important advances in our understanding of the structure and function of co-chaperones over the intervening period, we accepted the invitation. Indeed, the broader biological functions of co-chaperones are starting to emerge, as is our understanding of how theyactasnodestonetworkandfunctionalizechaperones.Inparticular,thebroader biological functions of these fascinating proteins suggest that their co-chaperone function may not always be their primary function. In the preface to the second editionofthebook,wedefinedaco-chaperoneas“anon-clientproteinthatinteracts with a protein chaperone and/or its client protein to regulate chaperone function”. Wewonderifthereisaneedtorevisethisnotionofaco-chaperone,tobettercapture how these proteins functionally network chaperone machinery into the cellular ecosystem?TheHsp40/DnaJproteinsareagoodexampleofaco-chaperonefamily whose biochemical and biological functions go well beyond the confines of this definition. This family exhibits considerable evolutionary radiation (especially in protozoan parasites!), with many more members than most other chaperone or co-chaperone families. In addition, many members are large proteins, with just the J domain (among many other domains) as evidence of their membership to the Hsp40/DnaJ family. Interestingly, it was recently proposed by a scientific consor- tiumofexpertsinthefieldthatthisfamilyofproteinsberenamedJ-domainproteins (JDPs),andthisnomenclatureisstartingtogaintractionintheliterature(including our book). You will notice that the third edition has a completely new chapter addressing the exciting new theme of post-translational modification of co-chaperones and the contribution to the chaperone code. Furthermore, all the v vi Preface otherchaptersarenotsimplyupdatedchaptersbutsubstantiallyrefreshedcontribu- tions, providing critical insights into the current status of the field. Together, the chapterscomprehensivelycapturetherolesofthemajorco-chaperonefamiliesunder physiological and disease conditions, including the core and specialized co-chaperones of the major molecular chaperones Hsp70 and Hsp90, co-chaperones of chaperonins, and organelle-specific co-chaperone function. And so,itisourpleasuretopresenttoyouthethirdeditionofourbook,whichwetrust youwillenjoyreadingasmuchaswehaveenjoyedfacilitatingitscreation. Grahamstown,SouthAfrica AdrienneL.Edkins Sharjah,UAE GregoryL.Blatch Acknowledgements We would like to acknowledge everyone who played a role in this fascinating and creative book project. This high-quality third edition of our book would not have beenarealitywithouttheexcellentongoingcommitmentofthepreviousauthorsand the insightful contributions of all the new authors and the reviewers. We also received tremendous support from Nature Springer in the planning and rolling out ofthisbookproject.Inparticular,wearegratefultoDr.MiriamSturm,whoalways providedprompt,expertadvice,andguidance,includingrobustoversightofthepeer reviewoftheeditor’schapters.Aswiththeprevioustwoeditionsofthebook,wedid not compromise on ensuring rigorous peer review of the chapters; however, given the COVID-19 context, the peer review process took longer than we anticipated. Hence,wewouldliketothankeveryonefortheirpatienceateachstageofthebook production. vii Contents 1 NucleotideExchangeFactorsforHsp70MolecularChaperones: GrpE,Hsp110/Grp170,HspBP1/Sil1,andBAG DomainProteins. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1 AndreasBracherandJacobVerghese 2 FunctionsoftheHsp90-BindingFKBPImmunophilins. . . . . . . . . . 41 NinaR.Ortiz,NaihsuanGuy,YenniA.Garcia,JeffreyC.Sivils, MarioD.Galigniana,andMarcB.Cox 3 Hsp70/Hsp90OrganisingProtein(Hop):CoordinatingMuch MorethanChaperones. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 81 KellySchwarz,SwatiBaindur-Hudson,GregoryLloydBlatch, andAdrienneLesleyEdkins 4 SpecificationofHsp70FunctionbyHsp40Co-chaperones. . . . . . .. 127 DouglasM.CyrandCarlosH.Ramos 5 Cdc37asaCo-chaperonetoHsp90. . . . . . . . . . . . . . . . . . . . . . . . . 141 ThomasL.Prince,BenjaminJ.Lang,YukaOkusha,TakanoriEguchi, andStuartK.Calderwood 6 p23andAha1:DistinctFunctionsPromoteClientMaturation. . .. 159 MaximilianM.BieblandJohannesBuchner 7 BeyondChaperoning:UCSProteinsEmergeasRegulators ofMyosin-MediatedCellularProcesses. . . . . . . . . . . . . . . . . . . . . . 189 OdutayoO.OdunugaandAndresF.Oberhauser 8 Chaperonin:Co-chaperoninInteractions. . . . . . . . . . . . . . . . . . . . 213 AileenBoshoff 9 Co-chaperonesoftheHumanEndoplasmicReticulum: AnUpdate. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 247 ArminMelnyk,SvenLang,MarkSicking,RichardZimmermann, andMartinJung ix x Contents 10 J-DomainProteinsOrchestratetheMultifunctionality ofHsp70sinMitochondria:InsightsfromMechanistic andEvolutionaryAnalyses. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 293 JaroslawMarszalek,ElizabethA.Craig,andBartlomiejTomiczek 11 ImpactofCo-chaperonesandPosttranslationalModifications TowardHsp90DrugSensitivity. . . . . . . . . . . . . . . . . . . . . . . . . . . 319 SarahJ.Backe,MarkR.Woodford,ElhamAhanin, RebeccaA.Sager,DimitraBourboulia,andMehdiMollapour 12 CHIP:ACo-chaperoneforDegradationbytheProteasome andLysosome. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 351 AbantikaChakrabortyandAdrienneL.Edkins 13 HSP70-HSP90ChaperoneNetworkinginProtein-Misfolding Disease. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 389 ChrisostomosProdromou,XaviAran-Guiu,JasmeenOberoi, LauraPerna,J.PaulChapple,andJacquelinevanderSpuy Index. . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 427