2018
PRRT2 Regulates Synaptic Fusion by Directly Modulating SNARE Complex Assembly
Coleman J, Jouannot O, Ramakrishnan SK, Zanetti MN, Wang J, Salpietro V, Houlden H, Rothman JE, Krishnakumar SS. PRRT2 Regulates Synaptic Fusion by Directly Modulating SNARE Complex Assembly. Cell Reports 2018, 22: 820-831. PMID: 29346777, PMCID: PMC5792450, DOI: 10.1016/j.celrep.2017.12.056.Peer-Reviewed Original ResearchConceptsProline-rich transmembrane protein 2SNARE complex assemblyComplex assemblyTrans-SNARE complex assemblyTerminal proline-rich domainSynaptic SNARE proteinsProline-rich domainParoxysmal neurological disordersSynaptic vesicle primingLive-cell imagingTransmembrane protein 2Synaptic fusionSNARE proteinsVesicle primingSingle exocytotic eventsBiophysical analysisFusion assaysMolecular mechanismsFunction mutationsPhysiological roleExocytotic eventsPre-synaptic terminalsPC12 cellsProtein 2Single vesicles
2017
The repeat region of cortactin is intrinsically disordered in solution
Li X, Tao Y, Murphy JW, Scherer AN, Lam TT, Marshall AG, Koleske AJ, Boggon TJ. The repeat region of cortactin is intrinsically disordered in solution. Scientific Reports 2017, 7: 16696. PMID: 29196701, PMCID: PMC5711941, DOI: 10.1038/s41598-017-16959-1.Peer-Reviewed Original ResearchConceptsCortactin repeatsRepeat regionActin filamentsHydrogen-deuterium exchange mass spectrometryAdjacent helical regionsMulti-domain proteinsExchange mass spectrometryExtensive biophysical analysisCircular dichroismHydrophobic core regionSmall-angle X-ray scatteringBiophysical analysisHelical regionCortactinRepeatsSimilar copiesUnfolded peptidesProteinMotifSize exclusion chromatographyMass spectrometryFilamentsExclusion chromatographyX-ray scatteringRegion
2015
bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles
Zheng H, Lee S, Llaguno MC, Jiang QX. bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles. Journal Of General Physiology 2015, 147: 77-93. PMID: 26712851, PMCID: PMC4692488, DOI: 10.1085/jgp.201511448.Peer-Reviewed Original ResearchConceptsMembrane proteinsIon channelsLipid compositionLipid bilayersMembrane systemLipid-protein interactionsVitro membrane systemSingle-molecule imagingVoltage-gated ion channelsGiant vesiclesUnilamellar naturePlanar electrodesPlanar lipid bilayersSuch proteinsMicroscopic imagingBiophysical analysisFast gating kineticsUnidirectional insertionProteinChannel activityProtein orientationGating kineticsModel systemBilayersSpecific ligands
2014
The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain
Rawling DC, Kohlway AS, Luo D, Ding SC, Pyle AM. The RIG-I ATPase core has evolved a functional requirement for allosteric stabilization by the Pincer domain. Nucleic Acids Research 2014, 42: 11601-11611. PMID: 25217590, PMCID: PMC4191399, DOI: 10.1093/nar/gku817.Peer-Reviewed Original ResearchConceptsATPase coreRetinoic acid-inducible gene IAcid-inducible gene INon-self RNASeries of mutationsActivity of RIGMetazoan cellsHelicase coreAllosteric controlTerminal domainPattern recognition receptorsAlpha-helixBiophysical analysisGene IAllosteric stabilizationType I interferonEnzymatic activityRecognition receptorsViral RNAStructural studiesRNAI interferonAdjacent domainsDomainImportant role
2013
Oligomerization and higher‐order assembly contribute to sub‐cellular localization of a bacterial scaffold
Bowman GR, Perez AM, Ptacin JL, Ighodaro E, Folta‐Stogniew E, Comolli LR, Shapiro L. Oligomerization and higher‐order assembly contribute to sub‐cellular localization of a bacterial scaffold. Molecular Microbiology 2013, 90: 776-795. PMID: 24102805, PMCID: PMC3859194, DOI: 10.1111/mmi.12398.Peer-Reviewed Original ResearchConceptsSub-cellular localizationAmino acidsN-terminal 23 amino acidsDefective mutant proteinsAsymmetric cell divisionC-terminal 76 amino acidsC-terminal domainDimer of trimersCaulobacter crescentusCell polesLocalization determinantsHigher-order structureMutant proteinsScaffold proteinSubcellular fociCell divisionLinker domainPopZMutational analysisBiophysical analysisWild typePolar organizationOrganizing centerDistinct setsProteinThe common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation
Harper SL, Sriswasdi S, Tang HY, Gaetani M, Gallagher PG, Speicher DW. The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. Blood 2013, 122: 3045-3053. PMID: 23974198, PMCID: PMC3811177, DOI: 10.1182/blood-2013-02-487702.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCross-Linking ReagentsElliptocytosis, HereditaryErythrocyte MembraneHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSpectrinConceptsHereditary elliptocytosisMembrane destabilizationLarge conformational rearrangementsGel filtration analysisMembrane proteinsTetramer assemblyHereditary pyropoikilocytosisBiophysical analysisCommon hereditary elliptocytosisConformational rearrangementsDimer conformationHelical contentTetramerization siteFiltration analysisSpectrin tetramersNovel mechanismUnknown mechanismMutationsBinding assaysSpectrinChemical crosslinkingErythrocyte shapeTetramerErythrocyte membranesMembrane
2001
Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation
Bian S, Favre I, Moczydlowski E. Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK channel involved in Ca2+-dependent activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 4776-4781. PMID: 11274367, PMCID: PMC31910, DOI: 10.1073/pnas.081072398.Peer-Reviewed Original ResearchConceptsIntracellular COOH-terminal domainDependent activationBK channelsCOOH-terminal domainProtein blot assayBiochemical approachesStructural basisBiophysical analysisBK proteinAsp residuesControl proteinHEK293 cellsEscherichia coliProteinElectrophysiological assaysBlot assaysLarge conductanceTerminal fragmentSoluble formActivationResiduesFunctional correlationSpecific bindingSpecific regionsBinding
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply