Karin Reinisch, PhD
Cards
About
Titles
David W. Wallace Professor of Cell Biology and of Molecular Biophysics and Biochemistry
Director of Graduate StudiesBiography
PhD in chemistry, under the direction of William N. Lipscomb. Post-doc under the direction of Stephen C. Harrison, Harvard University (1995-2001). Faculty at Yale since 2001.
Appointments
Cell Biology
ProfessorPrimaryMolecular Biophysics and Biochemistry
ProfessorSecondary
Other Departments & Organizations
- Biochemistry, Quantitative Biology, Biophysics and Structural Biology (BQBS)
- Cell Biology
- Cell Biology of RNA
- Cell Biology Research
- Center for RNA Science and Medicine
- Diabetes Research Center
- Membrane Traffic
- Molecular Biophysics and Biochemistry
- Molecular Cell Biology, Genetics and Development
- Reinisch Lab
- Structural Biology
- Yale Combined Program in the Biological and Biomedical Sciences (BBS)
- Yale Ventures
Education & Training
- PhD
- Harvard University (1995)
- BA
- Harvard-Radcliffe College (1989)
Research
Publications
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
2015
The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane
Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. Nature Cell Biology 2015, 18: 132-138. PMID: 26571211, PMCID: PMC4689616, DOI: 10.1038/ncb3271.Peer-Reviewed Original ResearchThe 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 activationMembraneRe-visiting the trans insertion model for complexin clamping
Krishnakumar SS, Li F, Coleman J, Schauder CM, Kümmel D, Pincet F, Rothman JE, Reinisch KM. Re-visiting the trans insertion model for complexin clamping. ELife 2015, 4: e04463. PMID: 25831964, PMCID: PMC4384536, DOI: 10.7554/elife.04463.Peer-Reviewed Original ResearchAdaptor Proteins, Vesicular TransportAlgorithmsAnimalsCalorimetryCircular DichroismEntropyFluorescence Resonance Energy TransferHumansKineticsMembrane FusionModels, NeurologicalMutationNerve Tissue ProteinsNeuronsProtein BindingSignal TransductionSNARE ProteinsSynaptic TransmissionSynaptotagminsVesicle-Associated Membrane Protein 2
2014
Sac1–Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus
Cai Y, Deng Y, Horenkamp F, Reinisch KM, Burd CG. Sac1–Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus. Journal Of Cell Biology 2014, 206: 485-491. PMID: 25113029, PMCID: PMC4137058, DOI: 10.1083/jcb.201404041.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsCatalysisCrystallography, X-RayEndoplasmic ReticulumGolgi ApparatusGreen Fluorescent ProteinsMembrane ProteinsModels, MolecularMultiprotein ComplexesPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsGolgi apparatusHomology domainRegulation of phosphatidylinositolN-terminal subdomainN-terminal portionPhosphoinositide phosphataseFamily proteinsSignal terminationEndoplasmic reticulumPhosphatidylinositolMembrane compositionSAC1Dual functionPhosphoinositideEffectorsPhosphataseAmyotrophic lateral sclerosisCharcot-MarieBroad distributionVps74OrthologuesTooth disordersGOLPH3MannosyltransferaseLateral sclerosisStructure 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 ResearchDiversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation
Langemeyer L, Bastos R, Cai Y, Itzen A, Reinisch KM, Barr FA. Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation. ELife 2014, 3: e01623. PMID: 24520163, PMCID: PMC3919270, DOI: 10.7554/elife.01623.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAspartic AcidBacterial ProteinsCatalytic DomainDeath Domain Receptor Signaling Adaptor ProteinsDNA-Binding ProteinsEnzyme ActivationGlutamineGuanine Nucleotide Exchange FactorsHeLa CellsHumansHydrolysisListeriaModels, MolecularMutagenesis, Site-DirectedMutationProtein ConformationRab GTP-Binding ProteinsRab1 GTP-Binding ProteinsRab5 GTP-Binding ProteinsSignal TransductionTransfectionConceptsActive site residuesGTP hydrolysis mechanismNucleotide-free formActive site glutamineSwitch II regionDifferent RabsRab activationRab GTPasesGTPase activationGlutamine mutantNucleotide exchangeGDP releaseRabActivation mechanismActivation pathwayActive formPathwayResiduesActivationII regionRAPlasticityGTPasesRab5GEF
Links & Media
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