Karin Reinisch, PhD
David W. Wallace Professor of Cell Biology and of Molecular Biophysics and BiochemistryCards
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Research
Publications
2025
ATG2 is a triglyceride transfer protein
Korfhage J, Elhan H, Wan N, Lu Y, Kauffmann L, Pilli G, Fuller D, Rios A, Reinisch K, Maddipati K, Thiam A, Melia T. ATG2 is a triglyceride transfer protein. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2517469122. PMID: 41296734, PMCID: PMC12685032, DOI: 10.1073/pnas.2517469122.Peer-Reviewed Original ResearchConceptsPhospholipid transportNeutral lipid triacylglycerolTransfer proteinLipid transfer proteinsTight bindingAmphipathic helixLipid triacylglycerolContact sitesSynthetic organellesTransfer phospholipidsStable bindingLipid dropletsAtg2Neutral lipidsATG2AMembrane structureLipid speciesProteinLipidPhospholipidsTriacylglycerolCellsMonolayerOrganellesBilayerKey challenges and recommendations for defining organelle membrane contact sites
Calì T, Bayer E, Eden E, Hajnóczky G, Kornmann B, Lackner L, Liou J, Reinisch K, Rhee H, Rizzuto R, Scorrano L, Brini M. Key challenges and recommendations for defining organelle membrane contact sites. Nature Reviews Molecular Cell Biology 2025, 26: 776-796. PMID: 40550870, DOI: 10.1038/s41580-025-00864-x.Peer-Reviewed Original ResearchMembrane contact sitesContact sitesContact site formationMembrane-bound compartmentsOrganelle interactionsTethering proteinsExtracellular stimuliCellular functionsCellular signalingSuper-resolution microscopyProteomic approachReporter constructsMolecular playersSite dynamicsOrganellesSite formationProteinPhysiological conditionsElectron tomographyExperimental approachExchange of ionsSitesPathological conditionsGeneticsMass spectrometryStructural clues about bridge-mediated lipid transfer
De Camilli P, Reinisch K. Structural clues about bridge-mediated lipid transfer. Nature Structural & Molecular Biology 2025, 32: 961-963. PMID: 40374928, DOI: 10.1038/s41594-025-01552-2.Peer-Reviewed Original ResearchVAC14 oligomerization is essential for the function of the FAB1/PIKfyve-VAC14-FIG4 complex.
Zhang L, Uygun T, Hahn H, Liu Y, Rivero-Ríos P, Li D, Navratna V, Bristow E, Luo G, Kovarzin A, Bo Y, Gadde S, Côté M, Ko D, Mosalaganti S, Reinisch K, Weisman L. VAC14 oligomerization is essential for the function of the FAB1/PIKfyve-VAC14-FIG4 complex. Molecular Biology Of The Cell 2025, 36: ar78. PMID: 40305106, PMCID: PMC12260172, DOI: 10.1091/mbc.e24-11-0490.Peer-Reviewed Original ResearchMeSH KeywordsCryoelectron MicroscopyFlavoproteinsHexosyltransferasesHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMutationPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesPhosphotransferases (Alcohol Group Acceptor)Protein BindingProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVesicular Transport ProteinsConceptsPatient mutationsFluorescence-detection size-exclusion chromatographyPI(3,5)P2Phosphatidylinositol 3,5-bisphosphatePull-down assaysMedium-resolution structureYeast mutationsPediatric neurodegenerative diseaseVac14Signaling lipidsCell lysatesMutationsOligomerizationNeurodegenerative diseasesElectron microscopy mappingKnockoutFab1/PIKfyveYeastEndosomesFIG4PIKfyveLysatesColocalizationComplexRegulationLipid Dynamics at Membrane Contact Sites
Reinisch K, De Camilli P, Melia T. Lipid Dynamics at Membrane Contact Sites. Annual Review Of Biochemistry 2025, 94: 479-502. PMID: 40067957, DOI: 10.1146/annurev-biochem-083024-122821.Peer-Reviewed Original ResearchConceptsContact sitesOrganelle contact sitesMembrane contact sitesIntegral membrane proteinsLipid transfer proteinsVesicular traffickingEndoplasmic reticulumLipid transferMembrane proteinsLipid movementOrganellesLipid transportTransfer proteinCellular membranesProteinBilayer asymmetryLipid dynamicsShedding new lightLipidMembranePhysiological mechanismsEukaryotesSitesReticulumTraffickingReconstitution approaches for understanding cellular lipid dynamics
Li D, Korfhage J, Reinisch K. Reconstitution approaches for understanding cellular lipid dynamics. Methods In Enzymology 2025 DOI: 10.1016/bs.mie.2025.11.022.Peer-Reviewed Original ResearchLipid transport proteinsEndoplasmic reticulumProtein-mediated lipid transferReconstitution approachFluorescence resonance energy transferFluorescence-based assayLipid dynamicsCytosolic leafletDynamics in vitroMembrane biogenesisPurified proteinResonance energy transferLipid transferRedistribution of lipidsLipid scramblaseScrambling activityLipid transportTransport proteinsProteinMechanistic studiesMolecular identityLipid bilayerLipidAssayArtificial membranes
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 interiorOrganellesReticulumPolypeptideTraffickingSpartin-mediated lipid transfer facilitates lipid droplet turnover
Wan N, Hong Z, Parson M, Korfhage J, Burke J, Melia T, Reinisch K. Spartin-mediated lipid transfer facilitates lipid droplet turnover. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2314093121. PMID: 38190532, PMCID: PMC10801920, DOI: 10.1073/pnas.2314093121.Peer-Reviewed Original Research
2021
The Role of VPS13 and Related Proteins in lipid transport at membrane contact sites
Reinisch K. The Role of VPS13 and Related Proteins in lipid transport at membrane contact sites. The FASEB Journal 2021, 35 DOI: 10.1096/fasebj.2021.35.s1.00089.Peer-Reviewed Original Research
2016
Control of plasma membrane lipid homeostasis by the extended synaptotagmins
Saheki Y, Bian X, Schauder CM, Sawaki Y, Surma MA, Klose C, Pincet F, Reinisch KM, De Camilli P. Control of plasma membrane lipid homeostasis by the extended synaptotagmins. Nature Cell Biology 2016, 18: 504-515. PMID: 27065097, PMCID: PMC4848133, DOI: 10.1038/ncb3339.Peer-Reviewed Original ResearchConceptsSMP domainE-Syt1ER-PM tethersMembrane lipid homeostasisPlasma membrane lipidsEndoplasmic reticulum proteinAccumulation of diacylglycerolE-SytsExtended synaptotagminsMolecular basisMajor glycerolipidsReticulum proteinsMetabolic recyclingMembrane lipidsLipid homeostasisPLC activationSynaptotagminSustained accumulationHomeostatic responseDiacylglycerolGlycerolipidsMetabolic changesGenomeCa2Accumulation
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