OK Protein prenylation and human diseases a balance of protein

OK Protein prenylation and human diseases a balance of protein

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时间:2019-08-06

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1、SCIENCECHINALifeSciencesSPECIALTOPIC:ModelanimalsandtheirapplicationsApril2015Vol.58No.4:328–335•REVIEW•doi:10.1007/s11427-015-4836-1Proteinprenylationandhumandiseases:abalanceofproteinfarnesylationandgeranylgeranylation*XUNa,SHENNing,WANGXiuXing,JIANGShan,XUEBin&LIC

2、haoJunMinistryofEducationKeyLaboratoryofModelAnimalsforDiseaseStudy,ModelAnimalResearchCenterandMedicalSchoolofNanjingUniversity,NationalResourceCenterforMutantMice,Nanjing210061,ChinaReceivedOctober27,2014;acceptedJanuary23,2015Theproteinprenylationisoneoftheessenti

3、alpost-translationalproteinmodifications,whichextensivelyexistsintheeukar-yocyte.Itincludesproteinfarnesylationandgeranylgeranylation,usingfarnesylpyrophosphate(FPP)orgeranylgeranylpyro-phosphate(GGPP)asthesubstrate,respectively.Theprenylationoccursbycovalentaddition

4、ofthesetwotypesofisoprenoidstocysteineresiduesatornearthecarboxylterminusoftheproteinsthatpossessCaaXmotif,suchasRassmallGTPasefamily.Theattachmentofhydrophobicprenylgroupscananchortheproteinstointracellularmembranesandtriggerdownstreamcellsignalingpathway.Geranylger

5、anylbiphosphatesynthase(GGPPS)catalyzesthesynthesisof20-carbonGGPPfrom15-carbonFPP.TheabnormalexpressionofthisenzymewillaffecttherelativecontentofFPPandGGPP,andthusdisruptsthebalancebetweenproteinfarnesylationandgeranylgeranylation,whichparticipatesintovariousaspects

6、ofcellularphysiologyandpa-thology.Inthispaper,wemainlyreviewthepropertyofthisimportantproteinpost-translationalmodificationandresearchprogressinitsregulationofcigarettesmokeinducedpulmonarydisease,adipocyteinsulinsensitivity,theinflammationre-sponseofSertolicells,the

7、hepaticlipogenesisandthecardiachypertrophy.proteinprenylation,GGPP,FPP,biologicalfunctionregulationCitation:XuN,ShenN,WangXX,JiangS,XueB,LiCJ.Proteinprenylationandhumandiseases:abalanceofproteinfarnesylationandgeranylgeranylation.SciChinaLifeSci,2015,58:328–335,doi:1

8、0.1007/s11427-015-4836-1Thepost-translationallipidmodificationofproteinshasoncethismodificationisdisrupted,whichaccountsforthebeenr

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