2022
Outer hair cell function is normal in βV spectrin knockout mice
Stankewich MC, Bai JP, Stabach PR, Khan S, Tan WJT, Surguchev A, Song L, Morrow JS, Santos-Sacchi J, Navaratnam DS. Outer hair cell function is normal in βV spectrin knockout mice. Hearing Research 2022, 423: 108564. PMID: 35864018, DOI: 10.1016/j.heares.2022.108564.Peer-Reviewed Original ResearchConceptsOuter hair cellsAuditory brainstem response wavesAuditory thresholdOuter hair cell functionSpiral ganglion neuronsEfferent nerve fibersHair cell functionNumber of afferentsGanglion neuronsNerve fibersKnockout miceNeuronal structuresMiceHair cellsCell functionElectromechanical activityPutative roleType IOngoing investigationExon deletionsSynaptopathyAfferentsData supportResponse wavesNeurons
2020
Catalysis‐Independent ENPP1 Protein Signaling Regulates Mammalian Bone Mass
Zimmerman K, Liu X, von Kroge S, Stabach P, Lester ER, Chu EY, Srivastava S, Somerman MJ, Tommasini SM, Busse B, Schinke T, Carpenter TO, Oheim R, Braddock DT. Catalysis‐Independent ENPP1 Protein Signaling Regulates Mammalian Bone Mass. Journal Of Bone And Mineral Research 2020, 37: 1733-1749. PMID: 35773783, PMCID: PMC9709593, DOI: 10.1002/jbmr.4640.Peer-Reviewed Original ResearchConceptsHeterotopic mineralizationBone massFibroblast growth factor 23Growth factor 23Low bone massSoft tissue calcificationEarly-onset osteoporosisFrizzled-related protein 1Soluble Wnt inhibitorsTrabecular bone microarchitectureENPP1 deficiencyΒ-catenin signalingFactor 23Plasma FGF23Vascular calcificationArterial calcificationNuclear β-cateninPlasma PPiBone microarchitectureMurine modelTissue calcificationPlasma PiWnt inhibitorsCalcificationMiceMusculoskeletal Comorbidities and Quality of Life in ENPP1‐Deficient Adults and the Response of Enthesopathy to Enzyme Replacement Therapy in Murine Models
Ferreira CR, Ansh AJ, Nester C, O'Brien C, Stabach PR, Murtada S, Lester ER, Khursigara G, Molloy L, Carpenter TO, Braddock DT. Musculoskeletal Comorbidities and Quality of Life in ENPP1‐Deficient Adults and the Response of Enthesopathy to Enzyme Replacement Therapy in Murine Models. Journal Of Bone And Mineral Research 2020, 37: 494-504. PMID: 34882836, PMCID: PMC9667476, DOI: 10.1002/jbmr.4487.Peer-Reviewed Original ResearchConceptsENPP1 deficiencyAsj/Musculoskeletal complicationsBrief Pain Inventory-Short FormPhysical Function Short FormFibroblast growth factor 23Achilles tendon calcificationHealth-related qualityMajority of patientsGrowth factor 23Cervical spine fusionPresence of enthesopathyQuality of lifeAnalgesic medicationRegular chowResidual painAdult patientsDose escalationFactor 23Replacement therapyPhysical functionCardiovascular calcificationTendon calcificationAchilles tendonSpine fusionResponse of the ENPP1‐Deficient Skeletal Phenotype to Oral Phosphate Supplementation and/or Enzyme Replacement Therapy: Comparative Studies in Humans and Mice
Ferreira CR, Kavanagh D, Oheim R, Zimmerman K, Stürznickel J, Li X, Stabach P, Rettig RL, Calderone L, MacKichan C, Wang A, Hutchinson HA, Nelson T, Tommasini SM, von Kroge S, Fiedler IA, Lester ER, Moeckel GW, Busse B, Schinke T, Carpenter TO, Levine MA, Horowitz MC, Braddock DT. Response of the ENPP1‐Deficient Skeletal Phenotype to Oral Phosphate Supplementation and/or Enzyme Replacement Therapy: Comparative Studies in Humans and Mice. Journal Of Bone And Mineral Research 2020, 36: 942-955. PMID: 33465815, PMCID: PMC8739051, DOI: 10.1002/jbmr.4254.Peer-Reviewed Original ResearchConceptsBone mineral densityLow bone mineral densityTrabecular bone massBone massEarly-onset osteoporosisAsj/Conventional therapyLower trabecular bone massGreater bone fragilityRisk of nephrocalcinosisHigh-phosphate dietLow bone massCortical bone massDevelopment of nephrocalcinosisBone biomechanical propertiesAcademic medical centerPlasma phosphorus concentrationsAutosomal recessive hypophosphatemic ricketsRecessive hypophosphatemic ricketsENPP1 deficiencyRachitic phenotypeMedullary nephrocalcinosisRenal failureNormal chowMineral densityImproving the Pharmacodynamics and In Vivo Activity of ENPP1‐Fc Through Protein and Glycosylation Engineering
Stabach PR, Zimmerman K, Adame A, Kavanagh D, Saeui CT, Agatemor C, Gray S, Cao W, De La Cruz EM, Yarema KJ, Braddock DT. Improving the Pharmacodynamics and In Vivo Activity of ENPP1‐Fc Through Protein and Glycosylation Engineering. Clinical And Translational Science 2020, 14: 362-372. PMID: 33064927, PMCID: PMC7877847, DOI: 10.1111/cts.12887.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArea Under CurveDisease Models, AnimalEnzyme Replacement TherapyGlycosylationHalf-LifeHistocompatibility Antigens Class IHumansMaleMice, TransgenicPhosphoric Diester HydrolasesProtein EngineeringProtein Structure, TertiaryPyrophosphatasesReceptors, FcRecombinant Fusion ProteinsVascular CalcificationConceptsProtein engineeringO-BuN-glycansGlycosylation engineeringCellular recyclingENPP1-deficient miceTerminal sialylationBiomanufacturing platformProtein therapeuticsCalcification disordersSialylationCellsVivo activityFc neonatal receptorTherapeuticsArterial calcificationProteinMurine modelManNAcEnzyme replacementNeonatal receptorEfficacious levelsGeneral strategyThree-prong strategyDrug potencyGenetic and pharmacologic modulation of cementogenesis via pyrophosphate regulators
Chu EY, Vo TD, Chavez MB, Nagasaki A, Mertz EL, Nociti FH, Aitken SF, Kavanagh D, Zimmerman K, Li X, Stabach PR, Braddock DT, Millán JL, Foster BL, Somerman MJ. Genetic and pharmacologic modulation of cementogenesis via pyrophosphate regulators. Bone 2020, 136: 115329. PMID: 32224162, PMCID: PMC7482720, DOI: 10.1016/j.bone.2020.115329.Peer-Reviewed Original Research
2019
Human Heterozygous ENPP1 Deficiency Is Associated With Early Onset Osteoporosis, a Phenotype Recapitulated in a Mouse Model of Enpp1 Deficiency
Oheim R, Zimmerman K, Maulding ND, Stürznickel J, von Kroge S, Kavanagh D, Stabach PR, Kornak U, Tommasini SM, Horowitz MC, Amling M, Thompson D, Schinke T, Busse B, Carpenter TO, Braddock DT. Human Heterozygous ENPP1 Deficiency Is Associated With Early Onset Osteoporosis, a Phenotype Recapitulated in a Mouse Model of Enpp1 Deficiency. Journal Of Bone And Mineral Research 2019, 35: 528-539. PMID: 31805212, PMCID: PMC7184798, DOI: 10.1002/jbmr.3911.Peer-Reviewed Original ResearchConceptsAutosomal recessive hypophosphatemic rickets type 2ENPP1 deficiencyEarly-onset osteoporosisGene-dose effectOnset osteoporosisAsj/Bone mineral density scansBone mineralization disturbancesRenal phosphate wastingCortical boneDose effectMild osteomalaciaMineralization disturbancesFGF23 levelsMild elevationPlasma FGF23Arterial calcificationBone massPhosphate wastingSkeletal manifestationsBone fragilityThoracic spineWild-type family membersType 2Adult men
2015
ENPP1-Fc prevents mortality and vascular calcifications in rodent model of generalized arterial calcification of infancy
Albright RA, Stabach P, Cao W, Kavanagh D, Mullen I, Braddock AA, Covo MS, Tehan M, Yang G, Cheng Z, Bouchard K, Yu ZX, Thorn S, Wang X, Folta-Stogniew EJ, Negrete A, Sinusas AJ, Shiloach J, Zubal G, Madri JA, De La Cruz EM, Braddock DT. ENPP1-Fc prevents mortality and vascular calcifications in rodent model of generalized arterial calcification of infancy. Nature Communications 2015, 6: 10006. PMID: 26624227, PMCID: PMC4686714, DOI: 10.1038/ncomms10006.Peer-Reviewed Original ResearchConceptsChronic kidney diseaseVascular calcificationArterial calcificationOrphan diseaseCommon diseaseSequelae of diseaseEctopic vascular calcificationInternal elastic laminaPrevent mortalityRenal failureCardiac failureKidney diseaseSubcutaneous administrationRodent modelsAnimal modelsEctopic calcificationVascular wallLarge arteriesElastic laminaDiseaseCalcificationCalciphylaxisDecreased concentrationSclerosisArtery
2011
Cell organization, growth, and neural and cardiac development require αII-spectrin
Stankewich MC, Cianci CD, Stabach PR, Ji L, Nath A, Morrow JS. Cell organization, growth, and neural and cardiac development require αII-spectrin. Journal Of Cell Science 2011, 124: 3956-3966. PMID: 22159418, PMCID: PMC3244980, DOI: 10.1242/jcs.080374.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAnkyrinsAxonsBody PatterningCarrier ProteinsCell MembraneCell PolarityCell ProliferationCraniofacial AbnormalitiesEmbryo, MammalianEmbryonic DevelopmentFemaleFibroblastsGene DeletionHeart Defects, CongenitalMaleMiceMice, Inbred C57BLMicrofilament ProteinsNeural Tube DefectsNeuroepithelial CellsPhenotypeProtein StabilityPseudopodiaSpectrinConceptsΑII-spectrinSteady-state protein levelsΒIII spectrinEmbryonic day 12.5Tissue patterningRenal epithelial cellsEmbryonic lethalCortical actinOrgan developmentAnkyrin BExon trappingEmbryonic fibroblastsTranscriptional levelΒ-spectrinCardiac developmentCell organizationCell spreadingAxon formationNeural tubeHeterozygous animalsTargeted disruptionApical membraneNeuroepithelial cellsDay 12.5Cell morphology
2010
Placental Viral Infection Sensitizes to Endotoxin‐Induced Pre‐Term Labor: A Double Hit Hypothesis
Cardenas I, Mor G, Aldo P, Lang SM, Stabach P, Sharp A, Romero R, Mazaki‐Tovi S, Gervasi M, Means RE. Placental Viral Infection Sensitizes to Endotoxin‐Induced Pre‐Term Labor: A Double Hit Hypothesis. American Journal Of Reproductive Immunology 2010, 65: 110-117. PMID: 20712808, PMCID: PMC3025809, DOI: 10.1111/j.1600-0897.2010.00908.x.Peer-Reviewed Original ResearchConceptsPre-term labourPre-term deliveryDouble-hit hypothesisViral infectionPregnancy outcomesBacterial infectionsCytokine/chemokine profilesHit hypothesisConcurrent bacterial infectionFetal immune responsePro-inflammatory cytokinesWild-type miceHuman primary trophoblastsMurine gammaherpesvirus 68Fetal deathChemokine profilesPoor prognosisPregnant womenAdverse outcomesPregnant miceLPS treatmentImmune responseBacterial productsPrimary trophoblastsLow doses
2008
Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells
Stabach PR, Devarajan P, Stankewich MC, Bannykh S, Morrow JS. Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells. American Journal Of Physiology - Cell Physiology 2008, 295: c1202-c1214. PMID: 18768923, PMCID: PMC2584975, DOI: 10.1152/ajpcell.00273.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnkyrin RepeatAnkyrinsCell PolarityChlorocebus aethiopsCOS CellsCytoplasmDogsEndoplasmic ReticulumGolgi ApparatusHumansMembrane GlycoproteinsMonomeric GTP-Binding ProteinsProtein ConformationProtein FoldingProtein Sorting SignalsProtein TransportRatsRecombinant Fusion ProteinsRNA InterferenceRNA, Small InterferingSodium-Potassium-Exchanging ATPaseTime FactorsTransfectionViral Envelope ProteinsConceptsEndoplasmic reticulumSecretory pathwayPlasma membraneVesicular stomatitis virus G proteinMadin-Darby canine kidney cellsVirus G proteinSmall hairpin RNACanine kidney cellsGolgi traffickingAnkyrin RGolgi transportSemipermeabilized cellsER retentionCytoplasmic domainMembrane proteinsAssembly pathwayProtein ankyrinIntracellular traffickingAnkyrinFusion proteinSimilar phenotypeG proteinsSuch phenotypesHairpin RNACultured cells
2006
A limited number of genes are involved in the differentiation of germinal center B cells
Nakayama Y, Stabach P, Maher SE, Mahajan MC, Masiar P, Liao C, Zhang X, Ye Z, Tuck D, Bothwell AL, Newburger PE, Weissman SM. A limited number of genes are involved in the differentiation of germinal center B cells. Journal Of Cellular Biochemistry 2006, 99: 1308-1325. PMID: 16795035, DOI: 10.1002/jcb.20952.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsB-LymphocytesCell DifferentiationCell LineChildChild, PreschoolDithiothreitolDNA-Binding ProteinsGene Expression ProfilingGerminal CenterHumansMolecular Sequence DataNuclear ProteinsOligonucleotide Array Sequence AnalysisPalatine TonsilProtein FoldingRegulatory Factor X Transcription FactorsTranscription FactorsTunicamycinX-Box Binding Protein 1ConceptsUnfolded protein responseX-box binding protein 1Interferon regulatory factor 4Protein 1B lymphocyte-induced maturation protein-1Transcription factor B lymphocyte-induced maturation protein-1Post-transcriptional changesBinding protein 1Maturation protein-1Mature B cellsDisulfide isomeraseTranscription factorsLevel of expressionPlasmacytoma cell lineProtein responseGene expressionRegulatory factor 4GenesGerminal center B cellsLymphoblastoid cellsLimited inductionCell linesB cellsFactor 4Germinal center centroblastsStimulation of Gαq-coupled M1 muscarinic receptor causes reversible spectrin redistribution mediated by PLC, PKC and ROCK
Street M, Marsh SJ, Stabach PR, Morrow JS, Brown DA, Buckley NJ. Stimulation of Gαq-coupled M1 muscarinic receptor causes reversible spectrin redistribution mediated by PLC, PKC and ROCK. Journal Of Cell Science 2006, 119: 1528-1536. PMID: 16551696, DOI: 10.1242/jcs.02872.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic Combined Chemotherapy ProtocolsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCricetinaeCyclophosphamideDoxorubicinGTP-Binding Protein alpha Subunits, Gq-G11Intracellular Signaling Peptides and ProteinsProtein Kinase CProtein Serine-Threonine KinasesReceptor, Muscarinic M1Receptors, MuscarinicRho-Associated KinasesSignal TransductionSpectrinType C PhospholipasesVincristineConceptsG protein-coupled receptorsAlphaII-spectrinSpecialized plasma membrane domainsPlasma membrane domainsIntact actin cytoskeletonStimulation of GPCRsProtein kinase CExtracellular stimuliActin cytoskeletonProtein complexesM1 muscarinic receptorsMembrane domainsMembrane blebbingPlasma membraneCytoskeletal proteinsKinase ROCKMolecular mechanismsConstitutive activationKinase CCellular localizationGlobal rearrangementsPhospholipase CSpectrinCHO cellsReversible redistributionHuman Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat
Stankewich MC, Stabach PR, Morrow JS. Human Sec31B: a family of new mammalian orthologues of yeast Sec31p that associate with the COPII coat. Journal Of Cell Science 2006, 119: 958-969. PMID: 16495487, DOI: 10.1242/jcs.02751.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsCarrier ProteinsCell LineCells, CulturedChlorocebus aethiopsCloning, MolecularCOP-Coated VesiclesCOS CellsExonsGene Expression RegulationHumansMolecular Sequence DataPhosphoproteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentVesicular Transport ProteinsConceptsCOPII coatProline-rich C-terminal regionEndoplasmic reticulumTerminal proline-rich regionCOPII vesicle coatVesicular tubular clustersProline-rich regionWD repeat domainFull-length proteinAlternative mRNA splicingN-terminal domainC-terminal regionVesicle coatWD repeatsMammalian orthologuesVesicular trafficSecretory pathwayMRNA splicingExon utilizationExon 13Sec31pChromosome 10q24Gene productsSec31BSpecialized functions
2005
Neutrophils Lacking Platelet-Endothelial Cell Adhesion Molecule-1 Exhibit Loss of Directionality and Motility in CXCR2-Mediated Chemotaxis
Wu Y, Stabach P, Michaud M, Madri JA. Neutrophils Lacking Platelet-Endothelial Cell Adhesion Molecule-1 Exhibit Loss of Directionality and Motility in CXCR2-Mediated Chemotaxis. The Journal Of Immunology 2005, 175: 3484-3491. PMID: 16148090, DOI: 10.4049/jimmunol.175.6.3484.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell ShapeChemokine CXCL1ChemokinesChemokines, CXCChemotaxis, LeukocyteCytokinesInterleukin-8Intracellular Signaling Peptides and ProteinsMiceMice, KnockoutNeutrophilsPlatelet Endothelial Cell Adhesion Molecule-1Protein Phosphatase 1Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesReceptors, Interleukin-8BConceptsCell motilitySrc homology 2 domainF-actinSHP-1 phosphatase activityWild-type neutrophilsF-actin polymerizationPhosphatase 1Time-lapse videomicroscopyPECAM-1Cytokine-induced mobilizationPhosphatase activityExhibit lossMurine neutrophilsMotilityChemotaxisZigmond chamberCellsPECAMLeading frontCytoskeletonMoesinIL-8FMLP gradientProteinActinExpression of ZER6 in ERα-Positive Breast Cancer
Stabach P, Thiyagarajan M, Weigel R. Expression of ZER6 in ERα-Positive Breast Cancer. Journal Of Surgical Research 2005, 126: 86-91. PMID: 15916980, DOI: 10.1016/j.jss.2005.02.006.Peer-Reviewed Original ResearchConceptsBreast cancerBreast carcinoma cellsERalpha-positive breast cancer cellsERalpha-negative breast cancersHormone-responsive breast cancerPrimary breast cancer tissuesERα-positive breast cancerERalpha-negative tumorsERalpha-positive tumorsCarcinoma cellsPrimary breast cancerERalpha-positive cell linesBreast cancer tissuesBreast cancer cellsERalpha expressionCancer tissuesCancerWestern blotRT-PCRCancer cellsLigand-dependent interactionCell linesTranscription factorsExpression of genesTumors
2000
βiv Spectrin, a New Spectrin Localized at Axon Initial Segments and Nodes of Ranvier in the Central and Peripheral Nervous System
Berghs S, Aggujaro D, Dirkx R, Maksimova E, Stabach P, Hermel J, Zhang J, Philbrick W, Slepnev V, Ort T, Solimena M. βiv Spectrin, a New Spectrin Localized at Axon Initial Segments and Nodes of Ranvier in the Central and Peripheral Nervous System. Journal Of Cell Biology 2000, 151: 985-1002. PMID: 11086001, PMCID: PMC2174349, DOI: 10.1083/jcb.151.5.985.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnkyrinsAutoantigensAxonsBlood ProteinsBrain ChemistryChromosomesCloning, MolecularCOS CellsCytoplasmCytoskeletonDiabetic NeuropathiesGene ExpressionHippocampusHumansIslets of LangerhansMaleMembrane ProteinsMiceMolecular Sequence DataNerve Tissue ProteinsPhosphoproteinsProtein Structure, TertiaryProtein Tyrosine PhosphatasesRanvier's NodesRatsRats, Sprague-DawleyReceptor-Like Protein Tyrosine Phosphatases, Class 8RNA, MessengerSciatic NerveSignal TransductionSodium ChannelsSpectrinConceptsPleckstrin homology domainHomology domainBetaIV spectrinActin-binding domainAxon initial segmentPutative SH3Alternative splicingSpectrin geneSpectrin repeatsDetergent extractabilityCell adhesion moleculeNodes of RanvierSubcellular fractionationTerminal halfAdditional isoformsDistinct isoformsLong isoformNorthern blotSpectrinAbundant expressionΒIV-spectrinIsoformsSpectrin antibodiesEmbryonic day 19Initial segmentIdentification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210
Stabach P, Morrow J. Identification and Characterization of βV Spectrin, a Mammalian Ortholog of Drosophila βHSpectrin* 210. Journal Of Biological Chemistry 2000, 275: 21385-21395. PMID: 10764729, DOI: 10.1074/jbc.c000159200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCloning, MolecularConsensus SequenceDNA, ComplementaryDrosophilaDrosophila ProteinsExonsGene LibraryHumansIntronsMammalsMolecular Sequence DataMolecular WeightOrgan SpecificityPhylogenyRatsRecombinant ProteinsRepetitive Sequences, Amino AcidRetinaSequence AlignmentSequence Homology, Amino AcidSpectrinTumor Cells, CulturedViral ProteinsConceptsDrosophila orthologMammalian orthologsSpectrin repeatsPleckstrin homology domainComplete cDNA sequenceActin-binding domainSelf-association domainAmino acids 85Amino acid sequenceBeta-spectrin geneHuman retina cDNA libraryRetina cDNA libraryFly counterpartMammalian spectrinsCaenorhabditis elegansHomology domainEpithelial cell populationsSH3 domainApical domainCDNA sequenceCDNA libraryOrthologsPolarized epitheliumBeta spectrinAcid sequence
1998
A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles
Stankewich M, Tse W, Peters L, Ch’ng Y, John K, Stabach P, Devarajan P, Morrow J, Lux S. A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 14158-14163. PMID: 9826670, PMCID: PMC24343, DOI: 10.1073/pnas.95.24.14158.Peer-Reviewed Original ResearchConceptsBetaIII spectrinGene mapsMembrane skeletonEndoplasmic reticulum marker calnexinPlasma membrane skeletonPleckstrin homology domainTrans-Golgi networkHuman brain cDNASyntenic regionsGene familyProtein 4.1Membrane associationCompartment markersImportant structural componentDa proteinSelf-association siteGolgi membranesHomology searchCDNA endsRapid amplificationUnidentified isoformChromosome 19Liver Golgi membranesGenBank databaseVesicle markersADP ribosylation factor regulates spectrin binding to the Golgi complex
Godi A, Santone I, Pertile P, Devarajan P, Stabach P, Morrow J, Di Tullio G, Polishchuk R, Petrucci T, Luini A, De Matteis M. ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 8607-8612. PMID: 9671725, PMCID: PMC21123, DOI: 10.1073/pnas.95.15.8607.Peer-Reviewed Original ResearchConceptsADP-ribosylation factorGolgi complexRibosylation factorG proteinsVesicular stomatitis virus G proteinPleckstrin homology domainSmall G proteinsPH domain interactionBinding of spectrinVirus G proteinGolgi spectrinHomology domainPH domainCoat proteinDocking siteDomain interactionsGolgiEndoplasmic reticulumPtdInsP2 levelsDomain IPhospholipase DSpectrinGolgi fractionsProteinPtdInsP2