2023
Dual regulation of SLC25A39 by AFG3L2 and iron controls mitochondrial glutathione homeostasis
Shi X, DeCiucis M, Grabinska K, Kanyo J, Liu A, Lam T, Shen H. Dual regulation of SLC25A39 by AFG3L2 and iron controls mitochondrial glutathione homeostasis. Molecular Cell 2023, 84: 802-810.e6. PMID: 38157846, PMCID: PMC10922821, DOI: 10.1016/j.molcel.2023.12.008.Peer-Reviewed Original ResearchProtein quality controlMitochondrial protein quality controlDual regulationMetabolic compartmentalizationIron homeostasisMitochondrial iron-sulfur clustersIron-sulfur clustersMitochondrial transportersProtein regulationMammalian cellsCRISPR knockoutCysteine residuesTransporter regulationLoop 1SLC25A39Glutathione homeostasisMetabolic sensingGlutathione uptakeMature neuronsProtein levelsHomeostasisRegulationAFG3L2Biochemical featuresMitochondrial glutathione levels
2019
APOBEC3A Loop 1 Is a Determinant for Single-Stranded DNA Binding and Deamination
Ziegler SJ, Hu Y, Devarkar SC, Xiong Y. APOBEC3A Loop 1 Is a Determinant for Single-Stranded DNA Binding and Deamination. Biochemistry 2019, 58: 3838-3847. PMID: 31448897, PMCID: PMC7211764, DOI: 10.1021/acs.biochem.9b00394.Peer-Reviewed Original ResearchConceptsSubstrate specificityLoop 1A3 proteinsRecent structural studiesBase editing technologyEnzyme catalytic polypeptideProtein functionSubstrate recognitionDNA bindingEditing technologySsDNA recognitionSubstrate selectionNovel CRISPRDeamination activityApolipoprotein B mRNACatalytic polypeptideBiochemical levelBase editorsLoop regionInnate immune systemProteinA3ADeaminase activityA3GA3 family
2000
Functional Role of Critical Stripe Residues in Transmembrane Span 7 of the Serotonin Transporter EFFECTS OF Na+, Li+, AND METHANETHIOSULFONATE REAGENTS*
Kamdar G, Penado K, Rudnick G, Stephan M. Functional Role of Critical Stripe Residues in Transmembrane Span 7 of the Serotonin Transporter EFFECTS OF Na+, Li+, AND METHANETHIOSULFONATE REAGENTS*. Journal Of Biological Chemistry 2000, 276: 4038-4045. PMID: 11058600, DOI: 10.1074/jbc.m008483200.Peer-Reviewed Original ResearchConceptsCys-109Methanethiosulfonate reagentsWater-filled poresNative cysteine residuesCysteine-containing mutantsExtracellular loop 1Close-contact regionThree-dimensional structureCysteine residuesTranslocation mechanismControl mutantsAlpha-helixMTSEA-biotinResidue positionsCysteine substitutionsLoop 1Conformational changesMTS reagentsFunctional roleMutantsIon bindingResiduesTransportersIon dependenceSerotonin transporter
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