2025
BPS2025 - Understanding recruitment mechanisms of peripheral membrane proteins: A novel two-step activation of Bruton's tyrosine kinase
McAllister R, Bhattacharyya M, Gupta K. BPS2025 - Understanding recruitment mechanisms of peripheral membrane proteins: A novel two-step activation of Bruton's tyrosine kinase. Biophysical Journal 2025, 124: 436a. DOI: 10.1016/j.bpj.2024.11.2330.Peer-Reviewed Original ResearchPeripheral membrane proteinsMembrane proteinsTyrosine kinaseActivation of Bruton's tyrosine kinaseBruton's tyrosine kinase
2024
Determining the membrane recruitment mechanisms of peripheral membrane proteins through native mass spectrometry directly from tunable lipid membranes
McAllister R, Jung W, Bhattacharyya M, Gupta K. Determining the membrane recruitment mechanisms of peripheral membrane proteins through native mass spectrometry directly from tunable lipid membranes. Biophysical Journal 2024, 123: 90a. DOI: 10.1016/j.bpj.2023.11.665.Peer-Reviewed Original ResearchNative mass spectrometryMass spectrometryMembrane recruitment mechanismPeripheral membrane proteinsLipid membranesSpectrometry
2018
Membrane shape-mediated wave propagation of cortical protein dynamics
Wu Z, Su M, Tong C, Wu M, Liu J. Membrane shape-mediated wave propagation of cortical protein dynamics. Nature Communications 2018, 9: 136. PMID: 29321558, PMCID: PMC5762918, DOI: 10.1038/s41467-017-02469-1.Peer-Reviewed Original ResearchConceptsMembrane shape changesF-BAR proteinsDomain-containing proteinsPeripheral membrane proteinsProtein lateral diffusionActin machineryProtein recruitmentMembrane proteinsProtein dynamicsCortical proteinsShape changesProtein waveActin wavesUnderappreciated roleProteinMembrane undulationsLateral diffusionSpatial gradientsMachineryCytoplasmImmune cellsRecruitmentAssemblyCells
2017
Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes
Hoogerheide D, Noskov S, Jacobs D, Bergdoll L, Silin V, Worcester D, Abramson J, Nanda H, Rostovtseva T, Bezrukov S. Structural features and lipid binding domain of tubulin on biomimetic mitochondrial membranes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e3622-e3631. PMID: 28420794, PMCID: PMC5422764, DOI: 10.1073/pnas.1619806114.Peer-Reviewed Original ResearchConceptsMitochondrial outer membraneMitochondrial membraneOuter membraneDimeric tubulinPeripheral membrane proteinsMembrane-binding domainOuter mitochondrial membraneDomain of tubulinIntegral proteinsMembrane proteinsCytosolic proteinsPhysiological roleHelix H10TubulinLipid headgroupsProteinComplex mechanismsMembranePeripheral bindingStructural featuresEssential stepCytoskeletonElectrochemical impedance spectroscopyMitochondriaDomain
2016
Syntabulin regulates the trafficking of PICK1-containing vesicles in neurons
Xu J, Wang N, Luo J, Xia J. Syntabulin regulates the trafficking of PICK1-containing vesicles in neurons. Scientific Reports 2016, 6: 20924. PMID: 26868290, PMCID: PMC4751430, DOI: 10.1038/srep20924.Peer-Reviewed Original ResearchMeSH KeywordsAcid Sensing Ion ChannelsAnimalsAxonsCarrier ProteinsChlorocebus aethiopsCOS CellsCytoskeletal ProteinsGene Knockdown TechniquesHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMicrotubule-Associated ProteinsMicrotubulesNeuronsNuclear ProteinsProtein BindingProtein TransportRatsTransport VesiclesConceptsMembrane proteinsKinesin-binding proteinPeripheral membrane proteinsDiverse membrane proteinsVesicle traffickingGolgi complexSyntabulinMembrane localizationSynaptic vesiclesTrafficking dynamicsMicrotubule structurePICK1TraffickingPICK1 expressionMetabotropic glutamate receptor 7VesiclesProteinMicrotubulesProtein expressionCell systemExpressionGolgiMitochondriaSynaptic receptorsReceptors
2011
Distinct Roles for F-BAR Proteins Cdc15p and Bzz1p in Actin Polymerization at Sites of Endocytosis in Fission Yeast
Arasada R, Pollard TD. Distinct Roles for F-BAR Proteins Cdc15p and Bzz1p in Actin Polymerization at Sites of Endocytosis in Fission Yeast. Current Biology 2011, 21: 1450-1459. PMID: 21885283, PMCID: PMC3350781, DOI: 10.1016/j.cub.2011.07.046.Peer-Reviewed Original ResearchConceptsF-BAR proteinsNucleation-promoting factorsActin patchesFission yeastArp2/3 complexActin polymerizationActin filamentsGenetic interaction experimentsSites of endocytosisPeripheral membrane proteinsActin binding proteinsClathrin-mediated endocytosisMembrane scissionYeast showSH3 domainCdc15pMembrane proteinsMembrane tubulesPlasma membraneGenetic analysisBinding proteinDistinct rolesEndocytosisProteinClathrin
2009
Imaging of the diffusion of single band 3 molecules on normal and mutant erythrocytes
Kodippili GC, Spector J, Sullivan C, Kuypers FA, Labotka R, Gallagher PG, Ritchie K, Low PS. Imaging of the diffusion of single band 3 molecules on normal and mutant erythrocytes. Blood 2009, 113: 6237-6245. PMID: 19369229, PMCID: PMC2699255, DOI: 10.1182/blood-2009-02-205450.Peer-Reviewed Original ResearchConceptsBand 3 moleculesBand 3Membrane componentsPeripheral membrane proteinsMembrane-spanning proteinsProtein-protein interactionsBand 3 populationMembrane proteinsSingle-particle trackingIntact human erythrocytesPlasma membraneIntact normal erythrocytesRed cell pathologyMotile propertiesDiseased cellsHuman erythrocyte membranesMutant erythrocytesCell pathologyProteinEntire complexHuman erythrocytesCompartment sizeErythrocyte membranesMembraneMembrane abnormalities
2003
Molecular Determinants of tGolgin-1 Function
Yoshino A, Marks M, Lemmon M. Molecular Determinants of tGolgin-1 Function. 2003 DOI: 10.21236/ada418143.Peer-Reviewed Original ResearchTrans-Golgi networkGRIP domainMammalian cellsC-terminal GRIP domainDynein/dynactin complexGRIP domain proteinsPeripheral membrane proteinsGTPase cascadeDomain proteinsDynactin complexGolgi networkMembrane proteinsCell motilityTurn bindsGolgi complexProtein resultsMolecular determinantsProteinTumor developmentOrthologuesCellsDomainRNAiEndosomesYeast
2002
Molecular Determinants of tGolgin-1 Function
Yoshino A, Marks M, Lemmon M. Molecular Determinants of tGolgin-1 Function. 2002 DOI: 10.21236/ada408101.Peer-Reviewed Original ResearchTrans-Golgi networkGRIP domainC-terminal GRIP domainGRIP domain proteinsPeripheral membrane proteinsN-terminal domainDomain proteinsGolgi networkTGN structureMammalian cellsGolgin-97Membrane proteinsCell motilityMolecular basisGolgi complexMolecular determinantsBroader roleCoil regionProteinTumor metastasisProtein contentCellsDomainRNAiMicrotubules
1997
Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *
Garcı́a-Cardeña G, Martasek P, Masters B, Skidd P, Couet J, Li S, Lisanti M, Sessa W. Dissecting the Interaction between Nitric Oxide Synthase (NOS) and Caveolin FUNCTIONAL SIGNIFICANCE OF THE NOS CAVEOLIN BINDING DOMAININ VIVO *. Journal Of Biological Chemistry 1997, 272: 25437-25440. PMID: 9325253, DOI: 10.1074/jbc.272.41.25437.Peer-Reviewed Original ResearchConceptsCaveolin-1Peripheral membrane proteinsInteraction of eNOSC-terminal tailAmino acids 310Direct interactionCo-transfection experimentsSite-directed mutagenesisNovel functional roleEndothelial nitric oxide synthaseMolecular chaperonesCytoplasmic domainCaveolin isoformsDeletion mutantsMammalian cellsEndothelial cell lysatesGlutathione S-transferaseMembrane proteinsCaveolin-2Coat proteinNegative regulationCaveolin-3Endothelial cellsDirect bindingGolgi regionActin-binding membrane proteins identified by F-actin blot overlays.
Luna E, Pestonjamasp K, Cheney R, Strassel C, Lu T, Chia C, Hitt A, Fechheimer M, Furthmayr H, Mooseker M. Actin-binding membrane proteins identified by F-actin blot overlays. Society Of General Physiologists Series 1997, 52: 3-18. PMID: 9210216.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActinsAmino Acid SequenceAnimalsBlotting, WesternBrainBreast NeoplasmsCattleChick EmbryoDictyosteliumElectrophoresis, Polyacrylamide GelHeLa CellsHumansIodine RadioisotopesMammalsMembrane ProteinsMiceMicrofilament ProteinsNeuroblastomaNeuropeptidesNeutrophilsSodium Dodecyl SulfateTumor Cells, CulturedConceptsBlot overlayApparent molecular massMembrane proteinsF-actinF-actin binding proteinMolecular massControl cell shapePeripheral membrane proteinsSpecialized membrane domainsCell-cell adhesionPlasma membrane-enriched fractionActin-binding proteinsMammalian cell linesCell surface extensionsMembrane-enriched fractionMembrane rufflesProtein 4.1Membrane domainsMammalian cellsDictyostelium discoideumSoil amoebaPseudopod dynamicsCell shapeEfficient chemotaxisMembrane bilayer
1994
Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C
Li C, Takei K, Geppert M, Daniell L, Stenius K, Chapman E, Jahn R, De Camilli P, Südhof T. Synaptic targeting of rabphilin-3A, a synaptic vesicle Ca2+/phospholipid-binding protein, depends on rab3A/3C. Neuron 1994, 13: 885-898. PMID: 7946335, DOI: 10.1016/0896-6273(94)90254-2.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsBase SequenceBiological EvolutionBrain ChemistryConserved SequenceDNA, ComplementaryFluorescent Antibody TechniqueGlutathione TransferaseGTP-Binding ProteinsMiceMice, Mutant StrainsMicroscopy, ImmunoelectronMolecular Sequence DataNerve Tissue ProteinsNeuronsrab GTP-Binding Proteinsrab3 GTP-Binding ProteinsRatsRecombinant Fusion ProteinsVesicular Transport ProteinsConceptsGTP-dependent mannerSynaptic vesicle membraneRabphilin-3AVesicle membraneLow molecular weight GTPPeripheral membrane proteinsSynaptic vesiclesSynaptic vesicle dockingRab3A-deficient miceSynaptic vesicle proteinsMembrane recruitmentVesicle dockingPutative functionsMembrane proteinsWeight GTPVesicle proteinsN-terminusSynaptic targetingRab3CRab3AProteinVesiclesMembraneSynaptic patternsNormal levels
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