SLC30A3 (ZnT3) Oligomerization by Dityrosine Bonds Regulates Its Subcellular Localization and Metal Transport Capacity 英文参考文献.docVIP

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SLC30A3 (ZnT3) Oligomerization by Dityrosine Bonds Regulates Its Subcellular Localization and Metal Transport Capacity 英文参考文献.doc

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SLC30A3 (ZnT3) Oligomerization by Dityrosine Bonds Regulates Its Subcellular Localization and Metal Transport Capacity 英文参考文献

SLC30A3(ZnT3)OligomerizationbyDityrosineBonds RegulatesItsSubcellularLocalizationandMetal TransportCapacity GloriaSalazar1*,JuanM.Falcon-Perez3,RobertHarrison4,VictorFaundez2 1DivisonofCardiology,DepartmentofMedicine,EmoryUniversitySchoolofMedicine,Atlanta,Georgia,UnitedStatesofAmerica,2DepartmentofCellBiology,Emory University School of Medicine, Atlanta, Georgia, United States of America, 3Metabolomics Unit, CIC bioGUNE, CIBERehd, Bizkaia, Spain, 4Department of Computer Science,GeorgiaStateUniversity,Atlanta,Georgia,UnitedStatesofAmerica Abstract Non-covalent and covalent homo-oligomerization of membrane proteins regulates their subcellular localization and function. Here, we described a novel oligomerization mechanism affecting solute carrier family 30 member 3/zinc transporter 3 (SLC30A3/ZnT3). Oligomerization was mediated by intermolecular covalent dityrosine bonds. Using mutagenizedZnT3expressedinPC12cells, weidentifiedtwocritical tyrosineresidues necessaryfordityrosine-mediated ZnT3 oligomerization. ZnT3 carrying the Y372F mutation prevented ZnT3 oligomerization, decreased ZnT3 targeting to synaptic-likemicrovesicles(SLMVs),anddecreasedresistancetozinctoxicity.Strikingly,ZnT3harboringtheY357Fmutation behavedasa‘‘gain-of-function’’mutantasitdisplayedincreasedZnT3oligomerization,targetingtoSLMVs,andincreased resistancetozinctoxicity.SingleanddoubletyrosineZnT3mutantsindicatethatthepredominantdimericspeciesisformed betweentyrosine357and372.ZnT3tyrosinedimerizationwasdetectedundernormalconditionsanditwasenhancedby oxidative stress. Covalent species were also detected in other SLC30A zinc transporters localized in different subcellular compartments. These results indicate that covalent tyrosine dimerization of a SLC30A family member modulates its subcellular localization and zinc transport capacity. We propose that dityrosine-dependent membrane protein oligomerizationmayregulatethefunctionofdiversemembraneproteininnormalanddiseasestates. Citation:SalazarG