2025
Biallelic variants in the conserved ribosomal protein chaperone gene PDCD2 are associated with hydrops fetalis and early pregnancy loss
Landry-Voyer A, Holling T, Mis E, Hassani Z, Alawi M, Ji W, Jeffries L, Kutsche K, Bachand F, Lakhani S. Biallelic variants in the conserved ribosomal protein chaperone gene PDCD2 are associated with hydrops fetalis and early pregnancy loss. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2426078122. PMID: 40208938, PMCID: PMC12012559, DOI: 10.1073/pnas.2426078122.Peer-Reviewed Original ResearchMeSH KeywordsAbortion, SpontaneousAllelesAnimalsApoptosis Regulatory ProteinsFemaleHumansHydrops FetalisMaleMolecular ChaperonesPregnancyRibosomal ProteinsConceptsRibosomal RNA processingRNA processingNonimmune hydrops fetalisRibosomal biogenesis disordersNext generation sequencingRibosome biogenesisPregnancy lossPatient variantsMolecular chaperonesExome sequencingGeneration sequencingPDCD2Biallelic variantsGenetic variantsHydrops fetalisIndependent familiesIn vivo approachesAffected fetusMolecular causesPrimary fibroblastsDevelopmental defectsMonogenic disordersAssociated with hydrops fetalisUS5Early pregnancy lossInfection-relevant conditions dictate differential versus coordinate expression of Salmonella chaperones and cochaperones
Chan C, Mukai K, Groisman E. Infection-relevant conditions dictate differential versus coordinate expression of Salmonella chaperones and cochaperones. MBio 2025, 16: e00227-25. PMID: 40162747, PMCID: PMC12077118, DOI: 10.1128/mbio.00227-25.Peer-Reviewed Original ResearchConceptsInfection-relevant conditionsJ-domainProtein homeostasisChaperone DnaKCytoplasmic MgMolecular chaperonesNucleotide exchange factor GrpEChaperone trigger factorSigma factor RpoHProteins co-translationallyExpression of molecular chaperonesPreventing protein aggregationIncreased mRNA amountsPerturb protein homeostasisMRNA amountsCochaperone DnaJRpoH proteinCo-translationallyPost-translationallyCochaperoneExpressed genesFolded proteinsDnaKCoordinated expressionChaperoneDSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress
Alim S, Cheppali S, Pawar S, Swamy M. DSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress. Biochimica Et Biophysica Acta (BBA) - Proteins And Proteomics 2025, 1873: 141064. PMID: 39956303, DOI: 10.1016/j.bbapap.2025.141064.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEquidaeFibronectinsHeat-Shock Proteins, SmallMaleMolecular ChaperonesOxidative StressPhosphorylcholineSemenConceptsChaperone-like activitySeminal plasmaFibronectin type IITetramer to monomersSperm capacitationSurface hydrophobicityMolecular chaperonesClient proteinsHeat shock proteinsBiophysical studiesAlcohol dehydrogenaseOxidative stressPhysiological ligandsShock proteinsProteinHead group moietySHspsBinding of phosphorylcholineCholine phospholipidsBindingFibronectinDehydrogenaseChaperoneSpermMammalsA human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability
Lim B, Xu J, Wierzbicki I, Gonzalez C, Chen Z, Gonzalez D, Gao X, Goodman A. A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability. Cell Host & Microbe 2025, 33: 200-217.e24. PMID: 39909037, PMCID: PMC11931560, DOI: 10.1016/j.chom.2025.01.008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsBacteroidesGastrointestinal MicrobiomeHumansMiceMicrobial InteractionsMolecular ChaperonesProtein FoldingConceptsHuman gut microbesChaperone complexGut microbesCommunity dynamicsHuman gut bacteriumProtein folding abilityProtein folding capacityHuman gut microbiomeMicrobial community dynamicsGut metagenomesNeighboring bacteriaExpression strainGut bacteriumMammalian gutFitness advantageGut microbiomeAllelic variationGenetic characterizationPathogen-induced inflammationSubstrate aggregationAntagonistic interactionsMicrobesRecipient cellsGutNeighboring cells
2024
Cotranslational molecular condensation of cochaperones and assembly factors facilitates axonemal dynein biogenesis
Li Y, Xu W, Cheng Y, Djenoune L, Zhuang C, Cox A, Britto C, Yuan S, Wang S, Sun Z. Cotranslational molecular condensation of cochaperones and assembly factors facilitates axonemal dynein biogenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2402818121. PMID: 39541357, PMCID: PMC11588059, DOI: 10.1073/pnas.2402818121.Peer-Reviewed Original ResearchMeSH KeywordsAxonemal DyneinsAxonemeChlamydomonas reinhardtiiMolecular ChaperonesProtein BiosynthesisRNA, MessengerConceptsDynein axonemal assembly factorsAssembly factorsCytosolic fociOuter dynein armsMacromolecular machinesAxonemal dyneinsAssembly hubDynein armsMolecular condensateLiquid-liquid phase separationCochaperoneEncoding mRNAFoci formationCiliary motilityStable interactionLRRC6Functional significanceRUVBL1DyneinMRNAAssembly of multiple componentsAssemblyPotential mechanismsRUVBL2BiogenesisChaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis
Chan C, Groisman E. Chaperone Hsp70 helps Salmonella survive infection-relevant stress by reducing protein synthesis. PLOS Biology 2024, 22: e3002560. PMID: 38574172, PMCID: PMC10994381, DOI: 10.1371/journal.pbio.3002560.Peer-Reviewed Original ResearchMeSH KeywordsBacteriaEscherichia coliEscherichia coli ProteinsHSP70 Heat-Shock ProteinsMagnesiumMolecular ChaperonesProtein FoldingSalmonellaConceptsRibosome associationProtein synthesisProtein homeostasisS. typhimuriumProtein folding capacityPreventing protein aggregationC-terminal amino acidsDomains of lifeProtein synthesis in vitroInhibit protein synthesisFolding capacityHsp70 chaperonesJ-domainSynthesis in vitroProtein foldingReduction of protein synthesisChaperone Hsp70DnaKRibosomeProtein aggregationChaperoneAmino acidsProteinStarvationHSP70
2023
ER chaperones use a protein folding and quality control glyco-code
Guay K, Ke H, Canniff N, George G, Eyles S, Mariappan M, Contessa J, Gershenson A, Gierasch L, Hebert D. ER chaperones use a protein folding and quality control glyco-code. Molecular Cell 2023, 83: 4524-4537.e5. PMID: 38052210, PMCID: PMC10790639, DOI: 10.1016/j.molcel.2023.11.006.Peer-Reviewed Original ResearchDiacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles
Li F, Grushin K, Coleman J, Pincet F, Rothman J. Diacylglycerol-dependent hexamers of the SNARE-assembling chaperone Munc13-1 cooperatively bind vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2306086120. PMID: 37883433, PMCID: PMC10623011, DOI: 10.1073/pnas.2306086120.Peer-Reviewed Original ResearchATR protects centromere identity by promoting DAXX association with PML nuclear bodies
Trier I, Black E, Joo Y, Kabeche L. ATR protects centromere identity by promoting DAXX association with PML nuclear bodies. Cell Reports 2023, 42: 112495. PMID: 37163376, DOI: 10.1016/j.celrep.2023.112495.Peer-Reviewed Original ResearchMeSH KeywordsCentromereCentromere Protein AHistonesMolecular ChaperonesPromyelocytic Leukemia Nuclear BodiesConceptsCentromere identityInterphase centromeresNuclear bodiesDNA damage-independent mannerPromyelocytic leukemia nuclear bodiesMitotic chromosome segregationCentromere protein AATR inhibitionDNA damage responsePML nuclear bodiesATR-dependent phosphorylationAcute ATR inhibitionChaperone DAXXGenome stabilityChromosome segregationPML-NBsDamage responseUnperturbed cellsMaster regulatorAtaxia telangiectasiaC-terminusFormation defectsCentromeresCENPAberrant increaseViral Evolution Shaped by Host Proteostasis Networks
Yoon J, Patrick J, Ogbunugafor C, Shoulders M. Viral Evolution Shaped by Host Proteostasis Networks. Annual Review Of Virology 2023, 10: 77-98. PMID: 37071930, PMCID: PMC10543606, DOI: 10.1146/annurev-virology-100220-112120.Peer-Reviewed Original ResearchConceptsProteostasis networkViral evolutionProtein foldingViral proteinsRegulate protein foldingViral protein productionEffective antiviral strategiesProteostasis factorsShape viral evolutionHost machineryAdaptive mutationsProtein biophysicsProtein productionFolding defectsAntiviral strategiesSequence spaceProteostasisProteinHostFoldingQuality control processChaperoneBiophysical defectsMutationsSequenceThe Histone Chaperone Network Is Highly Conserved in Physarum polycephalum
Poulet A, Rousselot E, Téletchéa S, Noirot C, Jacob Y, van Wolfswinkel J, Thiriet C, Duc C. The Histone Chaperone Network Is Highly Conserved in Physarum polycephalum. International Journal Of Molecular Sciences 2023, 24: 1051. PMID: 36674565, PMCID: PMC9864664, DOI: 10.3390/ijms24021051.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChromatinHistone ChaperonesHistonesMolecular ChaperonesPhysarum polycephalumSaccharomyces cerevisiaeConceptsHistone chaperonesEukaryotic treeChaperone networkBranching eukaryotesChaperone interactionsYeast complexCellular lifeDiverse proteinsPlant kingdomChaperone expressionRNA sequencingChaperonesKey residuesFunctional domainsHistonesCell cycleS phaseChromatinPhysarum polycephalumPlantsDistinct patternsEukaryotesOrthologuesCladeConserved
2022
A dynamic template complex mediates Munc18-chaperoned SNARE assembly
Yang J, Jin H, Liu Y, Guo Y, Zhang Y. A dynamic template complex mediates Munc18-chaperoned SNARE assembly. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2215124119. PMID: 36454760, PMCID: PMC9894263, DOI: 10.1073/pnas.2215124119.Peer-Reviewed Original ResearchMeSH KeywordsInsulinMembrane FusionMolecular ChaperonesQa-SNARE ProteinsSyntaxin 1Vesicle-Associated Membrane Protein 2ConceptsSoluble N-ethylmaleimide-sensitive factor attachment protein receptorsSNARE assemblyMunc18-3Munc18-1N-ethylmaleimide-sensitive factor attachment protein receptorsFactor attachment protein receptorsSNAP-25SNAP-25 bindingAttachment protein receptorsFour-helix bundleSynaptic vesicle fusionGlucose transporter translocationSNARE motifSNARE bundleSNAP-23Syntaxin 4GLUT4 translocationSyntaxin-1Transporter translocationPlasma membraneLinker regionMembrane fusionTemplate complexVesicle fusionMolecular mechanismsp97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells
Prophet SM, Naughton BS, Schlieker C. p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells. International Journal Of Molecular Sciences 2022, 23: 4627. PMID: 35563018, PMCID: PMC9100061, DOI: 10.3390/ijms23094627.Peer-Reviewed Original ResearchConceptsUbiquitylated proteinsNuclear pore complex assemblyPore complex assemblyNuclear envelope herniationsP97-dependent mannerP97 activityFG nucleoporinsComplex assemblyATPase deficiencyFG-NupsHeat shockHallmark phenotypeDYT1 dystoniaProteinAberrant depositionP97Therapeutic developmentDisease modelsUBXD1UbiquitylationBlebsK48UbiquitinHeterodimersUnexplored potentialLoss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass
Akel N, MacLeod R, Berryhill S, Laster D, Dimori M, Crawford J, Fu Q, Onal M. Loss of chaperone-mediated autophagy is associated with low vertebral cancellous bone mass. Scientific Reports 2022, 12: 3134. PMID: 35210514, PMCID: PMC8873216, DOI: 10.1038/s41598-022-07157-9.Peer-Reviewed Original ResearchConceptsProtein degradation pathwaysRole of CMACRISPR-Cas9-based genome editingChaperone-mediated autophagySkeletal homeostasisDegradation pathwayProteome remodelingMouse genomeGene trapCytoplasmic proteinsOsteoblastic cell lineGenome editingProteasomal degradationSpecific knockdownWild-type controlsCell typesLAMP2ACultured cellsOsteoblast formationCell linesRANKL expressionCathepsin K.Pathophysiological conditionsAutophagyCMA processThe endoplasmic reticulum proteostasis network profoundly shapes the protein sequence space accessible to HIV envelope
Yoon J, Nekongo E, Patrick J, Hui T, Phillips A, Ponomarenko A, Hendel S, Sebastian R, Zhang Y, Butty V, Ogbunugafor C, Lin Y, Shoulders M. The endoplasmic reticulum proteostasis network profoundly shapes the protein sequence space accessible to HIV envelope. PLOS Biology 2022, 20: e3001569. PMID: 35180219, PMCID: PMC8906867, DOI: 10.1371/journal.pbio.3001569.Peer-Reviewed Original ResearchMeSH KeywordsEndoplasmic ReticulumEndoplasmic Reticulum StressHIV InfectionsHumansMolecular ChaperonesProteostasisUnfolded Protein ResponseConceptsProteostasis networkUnfolded protein responseMutational toleranceHuman immunodeficiency virus-1Endoplasmic reticulumSequence spaceER proteostasis environmentProtein sequence spaceQuality control pathwaysHost endoplasmic reticulumER proteostasis networkChemical genetic strategySuites of chaperonesStress response pathwaysQuality control mechanismsEnv's mutational toleranceQuality control factorsRegion of envImmunodeficiency virus-1Proteostasis factorsEvolving proteinsProteostasis mechanismsProteostasis environmentCellular chaperonesIRE1-XBP1Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry
Simon B, Lou HJ, Huet-Calderwood C, Shi G, Boggon TJ, Turk BE, Calderwood DA. Tousled-like kinase 2 targets ASF1 histone chaperones through client mimicry. Nature Communications 2022, 13: 749. PMID: 35136069, PMCID: PMC8826447, DOI: 10.1038/s41467-022-28427-0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceCatalytic DomainCell Cycle ProteinsConserved SequenceCrystallography, X-RayHistonesHumansMolecular ChaperonesMolecular Docking SimulationMolecular MimicryMutagenesisPeptide LibraryPhosphorylationProtein KinasesRecombinant ProteinsSubstrate SpecificityConceptsTousled-like kinaseDNA replication-coupled nucleosome assemblyNuclear serine-threonine kinaseReplication-coupled nucleosome assemblyHistone chaperone proteinsGlobular N-terminal domainProper cell divisionPhosphorylation site motifsSerine-threonine kinaseShort sequence motifsAsf1 histone chaperonesC-terminal tailN-terminal domainHistone chaperonesGenome maintenanceNucleosome assemblySequence motifsChaperone proteinsNon-catalytic interactionsCatalytic domainCell divisionSite motifN-terminusStringent selectivityCell growth
2021
In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays.
Bobde R, Saharan K, Baral S, Gandhi S, Samal A, Sundaram R, Kumar A, Singh A, Datta A, Vasudevan D. In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays. Journal Of Visualized Experiments 2021 PMID: 35037657, DOI: 10.3791/63218.Peer-Reviewed Original ResearchConceptsHistone chaperonesH3/H4 tetramersNucleosome assembly processH3/H4H2A/H2BCore histones H2APull-down assaysAnalytical size exclusion chromatographyEukaryotic chromatinH4 tetramersHistone H2AH2A/Core histonesHistone octamerSingle copyChaperonesHistonesCellular cytoplasmDiverse classChromatinProteinDNAH2BH4Non-specific interactions
2020
CD44-Associated Tn Antigen as a New Biomarker of Tumor Cells with Aberrant Glycosylation
Shuvalova M, Kopylov A, Mazurov D, Pichugin A, Bovin N, Filatov A. CD44-Associated Tn Antigen as a New Biomarker of Tumor Cells with Aberrant Glycosylation. Biochemistry (Moscow) 2020, 85: 1064-1071. PMID: 33050853, DOI: 10.1134/s0006297920090060.Peer-Reviewed Original ResearchConceptsMucin 1O-glycosylationPairs of isogenic cell linesTumor-associated antigensTn antigenChimeric receptorsWild-type cellsProtein O-glycosylationIsogenic cell linesBiomarker of tumor cellsTreatment of tumorsA549 lung adenocarcinoma cellsAberrant O-glycosylationAnti-Tn antibodiesT-killersCosmc geneT cellsTumor cellsTumor growthCo-immunoprecipitationLung adenocarcinoma cellsDiagnosed tumorsWild typeTumorCancer cellsTorsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2
Rampello AJ, Laudermilch E, Vishnoi N, Prophet SM, Shao L, Zhao C, Lusk CP, Schlieker C. Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2. Journal Of Cell Biology 2020, 219: e201910185. PMID: 32342107, PMCID: PMC7265317, DOI: 10.1083/jcb.201910185.Peer-Reviewed Original ResearchConceptsNuclear pore biogenesisMyeloid leukemia factor 2FG nucleoporinsNuclear pore complex biogenesisNuclear envelope herniationsNuclear envelope reformationLive cell imaging platformProteomics-based approachNuclear envelope blebbingComplex biogenesisBleb formationUbiquitin conjugationNuclear envelopeATPase deficiencyBiogenesisHallmark phenotypePhenotypic hallmarksPOM121Factor 2Late markersLuminal componentsNup358CellsUbiquitinBlebbingThe Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease
Rampello AJ, Prophet SM, Schlieker C. The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease. Biomolecules 2020, 10: 468. PMID: 32204310, PMCID: PMC7175109, DOI: 10.3390/biom10030468.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDystoniaEndoplasmic ReticulumHSC70 Heat-Shock ProteinsHumansMolecular ChaperonesNuclear EnvelopeConceptsNuclear envelopeNuclear pore complex biogenesisEssential cellular processesNormal cellular physiologyNuclear envelope integrityDistinct subcellular localizationEndoplasmic reticulum networkCellular lipid metabolismTorsin ATPasesComplex biogenesisEnvelope integrityRegulatory cofactorsCellular physiologyCellular processesLuminal domainSubcellular localizationConsiderable medical importancePhenotypic consequencesCofactor assemblyTorsinsNE defectsATP hydrolysisReticulum networkDiverse processesPolypeptide 1
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