2025
The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation
Stacey J, Hrebík D, Nand E, Shetty S, Qu K, Boicu M, Anders-Össwein M, Uchil P, Dick R, Mothes W, Kräusslich H, Müller B, Briggs J. The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation. Nature 2025, 640: 258-264. PMID: 40011770, PMCID: PMC11964938, DOI: 10.1038/s41586-025-08624-9.Peer-Reviewed Original ResearchSpacer peptide 2Membrane-binding domainVirus particlesProtein-protein interfacesCleavage site mutantsHigh-resolution structuresFusion of virusImmature virus particlesHIV-1Site mutantsProteolytic cleavageFunctional domainsHuman immunodeficiency virus type 1Bound lipidsImmunodeficiency virus type 1Infectious virionsHIV-1 componentsStructural polyprotein GagMature latticeProtein latticeVirus type 1Structural maturationMonolayers in vitroPeptide 2Polyprotein Gag
2024
Mechanism of Negative Feedback Regulation of Oncogenic BCR-Signaling in Mature B-Cell Lymphoma
Sun R, Lee J, Robinson M, Kume K, Zhan C, Cheng Z, Cosgun K, Chan L, Leveille E, Kothari S, Katz S, Ma N, Vykunta V, Shy B, Hodson D, Marson A, Vaidehi N, Müschen M. Mechanism of Negative Feedback Regulation of Oncogenic BCR-Signaling in Mature B-Cell Lymphoma. Blood 2024, 144: 3003-3003. DOI: 10.1182/blood-2024-211693.Peer-Reviewed Original ResearchB-cell lymphomaGC B cellsB-cell lymphoma cellsB cellsBCR signalingGerminal centersProteolytic cleavageNK cellsLymphoma cellsMantle cell lymphoma xenograftsAggressive B-cell lymphomasMature B-cell lymphomasB-cell lymphoma subtypesGerminal center B cellsSpontaneous germinal centersGlobal phosphoproteomic studiesActivation marker CD69Aggressiveness of diseaseCD25 surface expressionMechanism of negative feedback regulationB cell autoimmunityFollicular dendritic cellsHuman germinal centerCa2+ oscillationsExpressed increased levels
2023
Pyroptosis in cardiovascular diseases: Pumping gasdermin on the fire
Yarovinsky T, Su M, Chen C, Xiang Y, Tang W, Hwa J. Pyroptosis in cardiovascular diseases: Pumping gasdermin on the fire. Seminars In Immunology 2023, 69: 101809. PMID: 37478801, PMCID: PMC10528349, DOI: 10.1016/j.smim.2023.101809.Peer-Reviewed Original ResearchConceptsPost-translational modificationsAcute cardiovascular eventsChronic cardiovascular diseaseCardiovascular diseaseSmall molecule inhibitorsPyroptosis resultsGenetic toolsGasdermin proteinsWhole organismInflammatory caspasesCardiovascular eventsCell deathMolecule inhibitorsCell typesProteolytic cleavageCellular mechanismsActivation of inflammasomesCardiovascular systemKnockout animalsAmplification of inflammationRole of pyroptosisPro-inflammatory processesDifferent cellsNovel therapeutic approachesPyroptosis
2019
Vasopressin inactivation: Role of insulin-regulated aminopeptidase
Li DT, Habtemichael EN, Bogan JS. Vasopressin inactivation: Role of insulin-regulated aminopeptidase. Vitamins & Hormones 2019, 113: 101-128. PMID: 32138946, DOI: 10.1016/bs.vh.2019.08.017.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsInsulin-regulated aminopeptidaseInsulin-responsive glucose transporterHuman placental leucine aminopeptidaseMetabolic syndromeInsulin resistanceVasopressin secretionUBX domainCoordinated regulationGenetic variationAbsence of insulinGLUT4 proteinGestational diabetes insipidusPotential pathophysiologic rolePhysiological importanceGlucose transporterCell surfaceProteolytic cleavageNovel insightsPlacental leucine aminopeptidaseRodent homologueVasopressinase activityLeucine aminopeptidasePathophysiologic mechanismsMuscle cellsPathophysiologic roleDifferential Influence of IL-9 and IL-17 on Actin Cytoskeleton Regulates the Migration Potential of Human Keratinocytes
Das S, Srinivasan S, Srivastava A, Kumar S, Das G, Das S, Dwivedi A, Karulkar A, Makkad K, Bilala R, Gupta A, Sawant A, Nayak C, Tayalia P, Purwar R. Differential Influence of IL-9 and IL-17 on Actin Cytoskeleton Regulates the Migration Potential of Human Keratinocytes. The Journal Of Immunology 2019, 202: 1949-1961. PMID: 30760620, DOI: 10.4049/jimmunol.1800823.Peer-Reviewed Original ResearchConceptsActin stress fibersHuman primary keratinocytesActomyosin machineryActomyosin cytoskeletonActin cytoskeletonCytoskeleton reorganizationStress fibersIncreased migration potentialMigration potentialRegulates numerous functionsMyosin L chainA-431 cellsHuman keratinocytesCellular contractilityProteolytic cleavageCytoskeletonSecreting specific cytokinesActomyosinIL-9Skin immune surveillanceActinMMP-independent mannerT cell cytokinesKeratinocyte migrationSkin homeostasis
2015
The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox
Kumar S, Stayrook S, Camire R, Krishnaswamy S. The X-Ray Structure of a Variant of Human Factor V Provides Structural Insights into the Procofactor Activation Paradox. Blood 2015, 126: 121. DOI: 10.1182/blood.v126.23.121.121.Peer-Reviewed Original ResearchB domainAcid regionC-terminusCofactor functionBR bindingDiffraction quality crystalsCoagulation factor VA3 domainFactor VaCofactor activityHomologous A domainsA1-A2-B-A3-C1-C2Ca2+-dependent fashionDomain organizationMolecular replacementAcid sequenceXa bindingSingle chain antibodyPrimary sequenceProteolytic excisionDevelopment of novel strategiesBind calcium ionsProteolytic processingProteolytic cleavageStructure-based model
2013
Polycystin-1 cleavage and the regulation of transcriptional pathways
Merrick D, Bertuccio CA, Chapin HC, Lal M, Chauvet V, Caplan MJ. Polycystin-1 cleavage and the regulation of transcriptional pathways. Pediatric Nephrology 2013, 29: 505-511. PMID: 23824180, PMCID: PMC3844055, DOI: 10.1007/s00467-013-2548-y.Peer-Reviewed Original ResearchConceptsAutosomal dominant polycystic kidney diseaseFluid-filled renal cystsPolycystin-2Transcriptional pathwaysPolycystin-1Primary ciliaProtein productsPhysiological functionsCommon genetic causeParent proteinProteolytic cleavageCleavage fragmentsGenetic causeGenesEnd-stage renal diseaseDominant polycystic kidney diseasePolycystic kidney diseaseBiological activityPathwayRenal diseaseKidney diseaseCleavageRenal parenchymaFragmentsRenal cysts
2011
Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions
Lal M, Caplan M. Regulated Intramembrane Proteolysis: Signaling Pathways and Biological Functions. Physiology 2011, 26: 34-44. PMID: 21357901, DOI: 10.1152/physiol.00028.2010.Peer-Reviewed Original ResearchConceptsFundamental cellular processesIntegral membrane proteinsFunctional protein domainsCellular processesProtein domainsElicit biological responsesMembrane proteinsTransmembrane proteinIntramembrane cleavageBiological functionsPhysiological processesProteolytic cleavageBiological responsesProteinCleavageDomainMessengerEnzymePathwayMembrane
2010
A STEP forward in neural function and degeneration
Baum ML, Kurup P, Xu J, Lombroso PJ. A STEP forward in neural function and degeneration. Communicative & Integrative Biology 2010, 3: 419-422. PMID: 21057629, PMCID: PMC2974069, DOI: 10.4161/cib.3.5.12692.Peer-Reviewed Original ResearchStriatal-enriched phosphataseProtein tyrosine phosphataseTyrosine kinase FynMAP kinases ERK1/2Tyrosine phosphataseKinase FynLocal translationKinases ERK1/2NR1/NR2BProteolytic cleavageNormal regulationNeurodegenerative diseasesSubunitsSynaptic plasticityPhosphataseRegulationGluR2 receptorsNR2B subunitSynaptic strengtheningUbiquitinationRecent progressNeural functionFynPhosphorylationGluR2 subunit
2007
Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*
Sánchez-Sánchez F, Martínez-Redondo F, Aroca-Aguilar JD, Coca-Prados M, Escribano J. Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*. Journal Of Biological Chemistry 2007, 282: 27810-27824. PMID: 17650508, DOI: 10.1074/jbc.m609608200.Peer-Reviewed Original ResearchConceptsExtracellular calciumCalpain IICalcium-activated proteaseIntraocular pressureT cellsIntracellular proteolytic cleavageCalpain inhibitorsCalcium uptakeProteolytic cleavageCalpain inhibitor IVOlfactomedin-like domainCalpain IInhibitor IVMyocilinEndoplasmic reticulumIntracellular processingLumenRNA interference knockdownCalciumProteolytic processingCellsCulture mediumGlaucomaSubcellular fractionationEndoproteolytic processingThe Phosphorylation State of GluR1 Subunits Determines the Susceptibility of AMPA Receptors to Calpain Cleavage*
Yuen EY, Liu W, Yan Z. The Phosphorylation State of GluR1 Subunits Determines the Susceptibility of AMPA Receptors to Calpain Cleavage*. Journal Of Biological Chemistry 2007, 282: 16434-16440. PMID: 17428797, DOI: 10.1074/jbc.m701283200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCalpainCells, CulturedCerebral CortexEnzyme ActivationNeuronsPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Processing, Post-TranslationalProtein SubunitsRatsRats, Sprague-DawleyReceptors, AMPATime FactorsConceptsCalpain cleavagePhosphorylation stateProteolytic cleavageDependent protein kinase IITerminal fusion proteinEffect of phosphorylationProtein phosphatase 1/2AProtein kinase IIPhosphorylation sitesProtein kinaseCalpain cleavage sitesGluR1 subunitKinase IIFusion proteinActive CaMKIIAMPAR currentsCalpain regulationCleavage siteIsoxazoleproprionic acid (AMPA) receptorSubunitsIonotropic glutamate receptorsN-methyl-D-aspartate receptorsPhysiological studiesExcitatory synaptic transmissionAMPA receptor currents
2004
Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus
Chauvet V, Tian X, Husson H, Grimm DH, Wang T, Hieseberger T, Igarashi P, Bennett AM, Ibraghimov-Beskrovnaya O, Somlo S, Caplan MJ. Mechanical stimuli induce cleavage and nuclear translocation of the polycystin-1 C terminus. Journal Of Clinical Investigation 2004, 114: 1433-1443. PMID: 15545994, PMCID: PMC525739, DOI: 10.1172/jci21753.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineCell NucleusChlorocebus aethiopsCHO CellsCOS CellsCricetinaeCricetulusDogsEmbryo, MammalianEpithelial CellsKidney TubulesMembrane ProteinsMiceMice, TransgenicPolycystic Kidney, Autosomal DominantProteinsSequence DeletionSignal TransductionStress, MechanicalTranscription Factor AP-1TRPP Cation ChannelsConceptsC-terminal tailAutosomal dominant polycystic kidney diseaseCell-matrix interactionsCiliary signalingSecond genePolycystin-2Polycystin-1C-terminusNovel pathwayProteolytic cleavageNuclear translocationMechanical stimuliGenesDominant polycystic kidney diseasePolycystic kidney diseasePrecise mechanismCleavageTerminusSignalingTranslocationNucleusPathway
2001
The CA 125 Gene: An Extracellular Superstructure Dominated by Repeat Sequences
O’Brien T, Beard J, Underwood L, Dennis R, Santin A, York L. The CA 125 Gene: An Extracellular Superstructure Dominated by Repeat Sequences. Tumor Biology 2001, 22: 348-366. PMID: 11786729, DOI: 10.1159/000050638.Peer-Reviewed Original ResearchConceptsThreonine-rich sequenceAmino acid repeat unitsShort cytoplasmic tailAmino-terminal domainRepeat unitsTransmembrane domainCytoplasmic tailRepeat domainTerminal domainO-glycosylationBiological functionsRepeat sequencesCytoplasmic phosphorylationEpitope binding sitesExtracellular domainExtracellular structuresCysteine loopProtein coreTransmembrane glycoproteinLarge transmembrane glycoproteinProteolytic cleavageGenesBinding sitesPhysiologic roleSequence
1997
Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain
Uellner R, Zvelebil M, Hopkins J, Jones J, MacDougall L, Morgan B, Podack E, Waterfield M, Griffiths G. Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain. The EMBO Journal 1997, 16: 7287-7296. PMID: 9405358, PMCID: PMC1170329, DOI: 10.1093/emboj/16.24.7287.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCytotoxicity, ImmunologicGlycosylationHexosaminidasesHumansIsoenzymesKiller Cells, NaturalLiposomesLymphocyte ActivationMembrane GlycoproteinsModels, MolecularMolecular Sequence DataPerforinPhospholipase C deltaPhospholipidsPore Forming Cytotoxic ProteinsProtein ConformationProtein Processing, Post-TranslationalRatsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTransfectionType C PhospholipasesConceptsC2 domainPro-pieceProteolytic cleavagePlasma membrane of target cellsBind phospholipid membranesMembrane of target cellsCalcium-dependent mannerSecreted proteinsIntracellular transportC-terminusPhospholipid membranesNK cell line YTPlasma membraneCleaved formInactive precursorAcidic compartmentsIncreased lytic activityConcanamycin AActive formLytic activityKilling assayE-64CleavageEpitope mappingPore formationα-Latrotoxin Stimulates Exocytosis by the Interaction with a Neuronal G-Protein-Coupled Receptor
Krasnoperov V, Bittner M, Beavis R, Kuang Y, Salnikow K, Chepurny O, Little A, Plotnikov A, Wu D, Holz R, Petrenko A. α-Latrotoxin Stimulates Exocytosis by the Interaction with a Neuronal G-Protein-Coupled Receptor. Neuron 1997, 18: 925-937. PMID: 9208860, DOI: 10.1016/s0896-6273(00)80332-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrain ChemistryCalciumCattleChromaffin GranulesCloning, MolecularCOS CellsDimerizationExocytosisGTP-Binding ProteinsMembrane ProteinsMolecular Sequence DataProtein PrecursorsQa-SNARE ProteinsRatsReceptors, Cell SurfaceReceptors, PeptideRecombinant ProteinsSensory Receptor CellsSequence AlignmentSequence Homology, Amino AcidSignal TransductionSpider VenomsTissue DistributionConceptsG protein-coupled receptorsAlpha-latrotoxin receptorNeuronal G protein-coupled receptorNovel orphan G-protein-coupled receptorI alphaCalcium-independent receptorSecretin receptor familyOrphan G protein-coupled receptorRegulation of neurosecretionEndogenous proteolytic cleavageMolecular cloningPrecursor polypeptideSerpentine receptorsCIRLFusion complexExtracellular bindingAlpha-LatrotoxinFunctional expressionReceptor familyProteolytic cleavagePresynaptic receptorsAffinity columnNeurotransmitter releaseStable complexesPresynaptic neurotoxins
1993
Poikilocytic Hereditary Elliptocytosis Associated With Spectrin Alexandria: An al/50b Kd Variant That Is Caused by a Single Amino Acid Deletion
Gallagher P, Roberts W, Benoit L, Speicher D, Marchesi S, Forget B. Poikilocytic Hereditary Elliptocytosis Associated With Spectrin Alexandria: An al/50b Kd Variant That Is Caused by a Single Amino Acid Deletion. Blood 1993, 82: 2210-2215. PMID: 8400271, DOI: 10.1182/blood.v82.7.2210.2210.Peer-Reviewed Original ResearchConceptsRed blood cellsHereditary elliptocytosisPolymerase chain reactionHeterogeneous disorderBlood cellsSingle amino acid deletionImpaired abilityDifferent severityChain reactionKD variantAffected individualsAlpha iAbnormal peptideAmino acid deletionSpectrin dimer self-associationProteolytic cleavage sitesResidues 470KD peptidePosition 470Limited tryptic digestionAcid deletionProteolytic cleavageErythrocyte membranesAmino acid sequence analysisIndividualsPoikilocytic hereditary elliptocytosis associated with spectrin Alexandria: an alpha I/50b Kd variant that is caused by a single amino acid deletion
Gallagher P, Roberts W, Benoit L, Speicher D, Marchesi S, Forget B. Poikilocytic hereditary elliptocytosis associated with spectrin Alexandria: an alpha I/50b Kd variant that is caused by a single amino acid deletion. Blood 1993, 82: 2210-2215. DOI: 10.1182/blood.v82.7.2210.bloodjournal8272210.Peer-Reviewed Original ResearchRed blood cellsHereditary elliptocytosisPolymerase chain reactionHeterogeneous disorderBlood cellsSingle amino acid deletionImpaired abilityDifferent severityChain reactionKD variantAffected individualsAlpha iAbnormal peptideAmino acid deletionSpectrin dimer self-associationProteolytic cleavage sitesResidues 470KD peptidePosition 470Limited tryptic digestionAcid deletionProteolytic cleavageErythrocyte membranesAmino acid sequence analysisIndividuals
1992
HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides
Riberdy J, Newcomb J, Surman M, Barbosat J, Cresswell P. HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides. Nature 1992, 360: 474-477. PMID: 1448172, DOI: 10.1038/360474a0.Peer-Reviewed Original ResearchConceptsClass II moleculesInvariant chainMajor histocompatibility complex (MHC) class II moleculesCell linesHLA-DR moleculesClass II binding siteInvariant chain peptideHLA-DR3 moleculesMore MHCClass IIAntigen processingT2 transfectantsAntigenic peptidesHuman cell linesChain peptideVivo conditionsPeptidesLarge proportionProteolytic cleavageMutant cell linesCertain human cell linesEarly stagesTransfectants
1991
Mitochondrial protein import.
Horwich A, Cheng M, West A, Pollock R. Mitochondrial protein import. Current Topics In Microbiology And Immunology 1991, 170: 1-42. PMID: 1760928, DOI: 10.1007/978-3-642-76389-2_1.Peer-Reviewed Original ResearchConceptsMitochondrial protein import pathwayProtein import pathwayPrecise molecular functionConformational alterationsImport pathwayMolecular functionsStep of recognitionMembrane translocationProteolytic cleavageProteinTranslocationDynamic picturePowerful toolGeneticsAlterationsPathwayBiochemistryCleavageCritical features
1989
Biosynthesis of a Phosphatidylinositol-Glycan-Linked Membrane Protein: Signals for Posttranslational Processing of the Ly-6E Antigen
Su B, Bothwell A. Biosynthesis of a Phosphatidylinositol-Glycan-Linked Membrane Protein: Signals for Posttranslational Processing of the Ly-6E Antigen. Molecular And Cellular Biology 1989, 9: 3369-3376. DOI: 10.1128/mcb.9.8.3369-3376.1989.Peer-Reviewed Original ResearchPhosphatidylinositol-glycanPhosphatidylinositol-glycan tailMutant proteinsLy-6Proteolytic cleavagePhosphatidylinositol glycan moietyPrimary translation productAmino acid sitesLy-6 proteinsCarboxy-terminal residuesTransient transfection proceduresCell surface proteinsMurine cell surface proteinLy-6 antigensCytoplasmic tailTranslation productsCleavage siteAsn residuesCOS cellsMembrane proteinsCOOH terminusPosttranslational processingPlasma membraneSurface proteinsTransmembrane form
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