2024
Lipid scrambling is a general feature of protein insertases
Li D, Rocha-Roa C, Schilling M, Reinisch K, Vanni S. Lipid scrambling is a general feature of protein insertases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2319476121. PMID: 38621120, PMCID: PMC11047089, DOI: 10.1073/pnas.2319476121.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsEndoplasmic reticulumMembrane proteinsPolypeptide chainLipid scramblingNascent polypeptide chainsVesicle traffickingBiochemical reconstitutionCytosolic leafletProtein insertionMembrane expansionInsertaseMembrane dynamicsHydrophilic grooveHydrophobic membrane interiorScramblaseProteinLipidMembraneBilayer leafletsMembrane interiorOrganellesReticulumPolypeptideTrafficking
2015
The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs
Horenkamp FA, Kauffman KJ, Kohler LJ, Sherwood RK, Krueger KP, Shteyn V, Roy CR, Melia TJ, Reinisch KM. The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs. Developmental Cell 2015, 34: 569-576. PMID: 26343456, PMCID: PMC4594837, DOI: 10.1016/j.devcel.2015.08.010.Peer-Reviewed Original ResearchConceptsATG8 proteinsIntracellular pathogen Legionella pneumophilaPre-autophagosomal structureAtg8/LC3 proteinsPathogen Legionella pneumophilaHigh-curvature membranesMembrane transport pathwaysCytosol of cellsEffector proteinsCatalytic domainHost cytosolRavZAutophagy proteinsLC3 proteinPathogenic microbesSubstrate affinityProteinIntermediate membraneLegionella pneumophilaAutophagosomesAutophagyCytosolTransport pathwaysInterfacial activationMembrane
2014
Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer
Schauder CM, Wu X, Saheki Y, Narayanaswamy P, Torta F, Wenk MR, De Camilli P, Reinisch KM. Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature 2014, 510: 552-555. PMID: 24847877, PMCID: PMC4135724, DOI: 10.1038/nature13269.Peer-Reviewed Original Research
2011
Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate
Wu X, Bradley MJ, Cai Y, Kümmel D, De La Cruz EM, Barr FA, Reinisch KM. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 18672-18677. PMID: 22065758, PMCID: PMC3219131, DOI: 10.1073/pnas.1110415108.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportCrystallography, X-RayDeath Domain Receptor Signaling Adaptor ProteinsGuanineGuanine Nucleotide Exchange FactorsHumansKineticsNucleotidesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRab GTP-Binding ProteinsRab1 GTP-Binding ProteinsConceptsGuanine nucleotide exchange factorsDENN domain proteinsMembrane traffic pathwaysNucleotide exchange factorsGDP-bound formGTP-bound formSwitch regions IHigher eukaryotesRab GTPasesGEF familyEukaryotic cellsTraffic pathwaysExchange factorSwitch INucleotide bindingKey regulatorConformational changesFirst structureNovel insightsRab35ProteinDENND1BEukaryotesRegion IGTPases
2010
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes
Vasan N, Hutagalung A, Novick P, Reinisch KM. Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 14176-14181. PMID: 20660722, PMCID: PMC2922553, DOI: 10.1073/pnas.1009419107.Peer-Reviewed Original ResearchConceptsGolgi-associated retrograde proteinC-terminusC-terminal fragmentGolgi-associated retrograde protein (GARP) complexCommon evolutionary originAlpha-helical bundleTrans-Golgi networkEndosome-derived vesiclesMembrane trafficVesicle recognitionEvolutionary originProtein complexesOligomeric GolgiTerminusSubunitsProteinComplexesDsl1ExocystFragmentsEndosomesGolgiFamilyMutationsVesicles
2006
Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen
Fuchs G, Stein AJ, Fu C, Reinisch KM, Wolin SL. Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen. Nature Structural & Molecular Biology 2006, 13: 1002-1009. PMID: 17041599, DOI: 10.1038/nsmb1156.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantigensBase SequenceBinding SitesCrystallography, X-RayModels, MolecularMolecular Sequence DataMutagenesisNuclease Protection AssaysNucleic Acid ConformationOocytesProtein BindingProtein Structure, TertiaryRibonucleoproteinsRNA 3' End ProcessingRNA PrecursorsRNA-Binding ProteinsRNA, Ribosomal, 5SXenopus laevis
2004
Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch
Dong G, Chakshusmathi G, Wolin SL, Reinisch KM. Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch. The EMBO Journal 2004, 23: 1000-1007. PMID: 14976553, PMCID: PMC380972, DOI: 10.1038/sj.emboj.7600115.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsAutoantigensConserved SequenceCrystallography, X-RayHelix-Turn-Helix MotifsHydroxylationModels, MolecularMolecular Sequence DataMutationPhosphatesProtein BindingProtein Structure, TertiaryRibonucleoproteinsRNASequence AlignmentSubstrate SpecificityTrypanosoma brucei bruceiConceptsLa motifLa proteinRNA polymerase III transcriptsFirst structural insightsRNA-binding proteinPolymerase III transcriptsHelix domainNuclear phosphoproteinRNA substratesMutagenesis experimentsStructural insightsConserved regionsHigh-affinity bindingAromatic patchHelix architectureProteinSurface residuesMotifRNAUridylateCritical roleTranscriptsPhosphoproteinExonucleaseFolding