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1、QuantitativeProteomicsRevealstheFunctionofUnconventionalUbiquitinChainsinProteasomalDegradationPingXu,1DucM.Duong,1NicholasT.Seyfried,1DongmeiCheng,1YangXie,2JessicaRobert,3JohnRush,4MarkHochstrasser,2DanielFinley,3andJunminPeng1,*1DepartmentofHumanGenetics,CenterforNeurod
2、egenerativeDiseases,EmoryUniversity,Atlanta,GA30322,USA2DepartmentofMolecularBiophysicsandBiochemistry,YaleUniversity,NewHaven,CT06520,USA3DepartmentofCellBiology,HarvardMedicalSchool,Boston,MA02115,USA4CellSignalingTechnology,Beverly,MA01915,USA*Correspondence:jpeng@emory
3、.eduDOI10.1016/j.cell.2009.01.041SUMMARYisreversiblethroughtheactionofdeubiquitinatingenzymes(DUBs).ThespecificityofUbsignalingismediatedbysubstrateAllsevenlysineresiduesinubiquitincontributetotherecognitionviatheE3ligases,theinteractionofUbmoietiessynthesisofpolyubiquitinc
4、hainsonprotein(monoUbandpolyUb)withUbreceptors,andUbremovalbysubstrates.WhereasK48-linkedchainsarewelles-specificDUBs.Morerecently,theregulationofUbpathwaystablishedasmediatorsofproteasomaldegradation,byUbchainsbearingdistinctpolyUblinkageshasemergedasandK63-linkedchainsact
5、innonproteolyticevents,animportantmechanism.ThesynthesisofparticularpolyUbchainlinkagesappearstobetherolesofunconventionalpolyubiquitinchainsafunctionofspecificE2sandtheE2-E3combinationsinvolvedlinkedthroughK6,K11,K27,K29,orK33arenot(Jinetal.,2008;Kimetal.,2007;Kirkpatricke
6、tal.,2006).Forwellunderstood.Here,wereportthattheunconven-example,theCdc34E2generatespredominantlyK48-linkedtionallinkagesareabundantinvivoandthatallnon-polyUbproducts,anditsspecificityisdependentonanacidicK63linkagesmaytargetproteinsfordegradation.loopregionofCdc34(Petrosk
7、iandDeshaies,2005).TheMms2/UbiquitinwithK48asthesinglelysinecannotsupportUbc13E2complexpreferentiallycatalyzestheformationofyeastviability,anddifferentlinkageshavepartiallypolyUbwithK63linkages,becausethestructureofMms2allowsredundantfunctions.Byprofilingboththeentireyeastf
8、orselectiveinsertionoftheK63sidechainofUbintotheUbc13proteomeandubiquitinatedproteinsinwi
