2025
WAVE complex forms linear arrays at negative membrane curvature to instruct lamellipodia formation
Wu M, Sadhu R, Meyer K, Tang Z, Marchando P, Woolfson D, Gov N, Weiner O. WAVE complex forms linear arrays at negative membrane curvature to instruct lamellipodia formation. Journal Of Cell Biology 2025, 224: e202410098. PMID: 40668190, PMCID: PMC12266138, DOI: 10.1083/jcb.202410098.Peer-Reviewed Original ResearchConceptsNucleation-promoting factorsNegative membrane curvatureLamellipodia formationActin nucleation-promoting factorMembrane curvatureIn vivo biochemical approachesSheet-like lamellipodiaActin-based protrusionsCell morphogenesisMembrane associationCell protrusionsBiochemical approachesUpstream activatorPlasma membraneLamellipodiaProtein arraysMechanistic basesLinear organizationWave complexesComplex patternsABI2WAVE2ActinLinear arrayMorphogenesis
2020
Scaffold association factor B (SAFB) is required for expression of prenyltransferases and RAS membrane association
Zhou M, Kuruvilla L, Shi X, Viviano S, Ahearn IM, Amendola CR, Su W, Badri S, Mahaffey J, Fehrenbacher N, Skok J, Schlessinger J, Turk BE, Calderwood DA, Philips MR. Scaffold association factor B (SAFB) is required for expression of prenyltransferases and RAS membrane association. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 31914-31922. PMID: 33257571, PMCID: PMC7749360, DOI: 10.1073/pnas.2005712117.Peer-Reviewed Original ResearchMeSH KeywordsAlkyl and Aryl TransferasesCell MembraneComputational BiologyCRISPR-Cas SystemsDatasets as TopicDimethylallyltranstransferaseGene Knockdown TechniquesHumansMatrix Attachment Region Binding ProteinsNeoplasmsNuclear Matrix-Associated ProteinsProtein PrenylationProtein SubunitsProto-Oncogene Proteins p21(ras)Receptors, EstrogenConceptsMembrane associationRAS membrane associationFarnesyltransferase inhibitorsPrenylation pathwayGenome-wide CRISPRGTP loadingAlternative prenylationMutant cellsNuclear proteinsKRAS membrane associationsRAS isoformsΑ-subunitGrowth inhibitionExpressionFactor BPathwayAnticancer therapyAlternative therapeutic strategiesPrenyltransferasesRasTherapeutic strategiesCRISPRFarnesyltransferaseMislocalizationPrenylationRetromer forms low order oligomers on supported lipid bilayers
Deatherage CL, Nikolaus J, Karatekin E, Burd CG. Retromer forms low order oligomers on supported lipid bilayers. Journal Of Biological Chemistry 2020, 295: 12305-12316. PMID: 32651229, PMCID: PMC7443500, DOI: 10.1074/jbc.ra120.013672.Peer-Reviewed Original ResearchConceptsLow-order oligomersAccessory factorsLipid bilayersMembrane-associated cargoesCoat protein complexIntegral membrane proteinsModel cargo proteinSingle-particle fluorescence microscopyRetromer sorting pathwayMembrane cargoNexin 3WASH complexCargo proteinsSorting pathwaysMembrane associationProtein complexesSNX3-retromerEndosomal systemMembrane proteinsEndosome membraneRecycling pathwayRetromerOligomeric interactionsIntrinsic propensityFluorescence microscopy
2015
Minimalist Model Systems Reveal Similarities and Differences between Membrane Interaction Modes of MCL1 and BAK*
Landeta O, Landajuela A, Garcia-Saez A, Basañez G. Minimalist Model Systems Reveal Similarities and Differences between Membrane Interaction Modes of MCL1 and BAK*. Journal Of Biological Chemistry 2015, 290: 17004-17019. PMID: 25987560, PMCID: PMC4505444, DOI: 10.1074/jbc.m114.602193.Peer-Reviewed Original ResearchConceptsBCL2 family proteinsFamily proteinsStructural foldMembrane environmentStable heterodimeric complexMembrane association modesFluorescence cross-correlation spectroscopyBCL2 family membersMembrane interaction modesCross-correlation spectroscopyCell fateMembrane associationHeterodimeric complexBCL2 familyMitochondrial membraneCellular factorsFluorescence-based techniquesMode of actionApoptosis-related factorsBakKey modulatorFRET measurementsMCL1ProteinCardiolipin content
2010
Kinase Associated-1 Domains Drive MARK/PAR1 Kinases to Membrane Targets by Binding Acidic Phospholipids
Moravcevic K, Mendrola JM, Schmitz KR, Wang YH, Slochower D, Janmey PA, Lemmon MA. Kinase Associated-1 Domains Drive MARK/PAR1 Kinases to Membrane Targets by Binding Acidic Phospholipids. Cell 2010, 143: 966-977. PMID: 21145462, PMCID: PMC3031122, DOI: 10.1016/j.cell.2010.11.028.Peer-Reviewed Original ResearchConceptsKA1 domainBud neck localizationMembrane association domainAcidic phospholipidsImportance of phosphatidylserineAssociation domainMembrane associationMembrane localizationProtein kinaseC2 domainC-terminusMembrane targetsKinaseIntact proteinAnionic phospholipidsX-ray crystallographyNeck localizationPhosphatidylserinePhospholipidsCrucial roleDomainMembrane surfaceLocalizationTerminusRegulatorChapter 136 Pleckstrin Homology (PH) Domains
Lemmon M. Chapter 136 Pleckstrin Homology (PH) Domains. 2010, 1093-1101. DOI: 10.1016/b978-0-12-374145-5.00136-4.Peer-Reviewed Original ResearchPleckstrin homology domainPH domainHomology domainPH domain-containing proteinsDifferent PH domainsDomain-containing proteinsReceptor-mediated endocytosisParticular phosphoinositidesMembrane traffickingMembrane associationProtein functionSequence similarityCommon foldCellular signalingCytoskeletal organizationFunctional relatednessProtein targetsPhosphoinositidePhysiological rolePhysiological relevancePromiscuous bindingX-ray crystallographyPhospholipid modificationStructural similarityProtein
2009
RSBP-1 Is a Membrane-targeting Subunit Required by the Gαq-specific But Not the Gαo-specific R7 Regulator of G protein Signaling in Caenorhabditis elegans
Porter MY, Koelle MR. RSBP-1 Is a Membrane-targeting Subunit Required by the Gαq-specific But Not the Gαo-specific R7 Regulator of G protein Signaling in Caenorhabditis elegans. Molecular Biology Of The Cell 2009, 21: 232-243. PMID: 19923320, PMCID: PMC2808233, DOI: 10.1091/mbc.e09-07-0642.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell MembraneGTP-Binding Protein alpha Subunits, Gi-GoGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding Protein RegulatorsImmunoprecipitationLocomotionMembrane ProteinsMolecular Sequence DataMusclesMutationNervous SystemOvulationProtein TransportRGS ProteinsSequence AlignmentSequence Homology, Amino AcidSignal TransductionSubcellular FractionsTransgenesConceptsR7 RGS proteinsRGS proteinsCaenorhabditis elegansEGL-10EAT-16G protein signaling (RGS) proteinsG proteinsMembrane-targeting sequenceGalpha GTPase activityC. elegans neuronsPhenocopies lossR7 regulatorMembrane associationRGS activityMembrane localizationProtein familyR7 familySignaling proteinsGTPase activityPlasma membraneGenetic studiesCultured cellsProteinR7BPElegansRho GDP Dissociation Inhibitor 2 Suppresses Metastasis via Unconventional Regulation of RhoGTPases
Moissoglu K, McRoberts KS, Meier JA, Theodorescu D, Schwartz MA. Rho GDP Dissociation Inhibitor 2 Suppresses Metastasis via Unconventional Regulation of RhoGTPases. Cancer Research 2009, 69: 2838-2844. PMID: 19276387, PMCID: PMC2701105, DOI: 10.1158/0008-5472.can-08-1397.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalscdc42 GTP-Binding ProteinCell AdhesionGuanine Nucleotide Dissociation InhibitorsHumansLung NeoplasmsMicerac1 GTP-Binding Proteinrho GTP-Binding Proteinsrho Guanine Nucleotide Dissociation Inhibitor betarho-Specific Guanine Nucleotide Dissociation InhibitorsrhoA GTP-Binding ProteinTumor Suppressor ProteinsUrinary Bladder NeoplasmsVinculinConceptsRho GTPasesFamily of proteinsGDP dissociation inhibitor 2Rho GDP dissociation inhibitor 2Dissociation inhibitor 2Membrane targetingMembrane associationPoint mutantsMetastasis suppressorRac1 activityGTPasesMetastasis suppressionInhibitor 2Suppress metastasisRhoGDI2ProteinSuppression correlatesRhoGDI1Weak inhibitorInhibitionRhoGTPasesMutantsMetastasis inhibitionStrong inhibitionSuppressor
2008
Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State
Das S, Stivison E, Folta-Stogniew E, Oliver D. Reexamination of the Role of the Amino Terminus of SecA in Promoting Its Dimerization and Functional State. Journal Of Bacteriology 2008, 190: 7302-7307. PMID: 18723626, PMCID: PMC2580686, DOI: 10.1128/jb.00593-08.Peer-Reviewed Original ResearchConceptsWild-type SecAProtein-conducting channelCell growthAmino-terminal regionSecA dimerSecA functionsProtein translocationSecA expressionMembrane associationMutant proteinsCell fractionationATPase specific activityCorresponding proteinProtein cargoCarboxyl terminusAmino terminusVivo functionSecADimerization defectFunctional stateMutantsBiochemical studiesResidue resultsProteinChemical crossEnzymological Analysis of Mutant Protein Kinase Cγ Causing Spinocerebellar Ataxia Type 14 and Dysfunction in Ca2+ Homeostasis*
Adachi N, Kobayashi T, Takahashi H, Kawasaki T, Shirai Y, Ueyama T, Matsuda T, Seki T, Sakai N, Saito N. Enzymological Analysis of Mutant Protein Kinase Cγ Causing Spinocerebellar Ataxia Type 14 and Dysfunction in Ca2+ Homeostasis*. Journal Of Biological Chemistry 2008, 283: 19854-19863. PMID: 18499672, DOI: 10.1074/jbc.m801492200.Peer-Reviewed Original ResearchConceptsCa2+-mediated signalingDomain mutantsMembrane residence timeEnzymological analysisIn vitro kinase assaySpinocerebellar ataxia type 14Total internal reflection fluorescence microscopyAutosomal dominant neurodegenerative diseaseDominant neurodegenerative diseaseSustained Ca2Bind diacylglycerolSingle molecule observationMembrane associationResponse to muscarinic receptor stimulationEnzymological propertiesKinase assayMutantsKinase activityC1 domainReceptor ligationPlasma membraneType 14Muscarinic receptor stimulationMediated signalingWild-type
2007
MAL decreases the internalization of the aquaporin-2 water channel
Kamsteeg EJ, Duffield AS, Konings IB, Spencer J, Pagel P, Deen PM, Caplan MJ. MAL decreases the internalization of the aquaporin-2 water channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 16696-16701. PMID: 17940053, PMCID: PMC2034241, DOI: 10.1073/pnas.0708023104.Peer-Reviewed Original ResearchConceptsAquaporin-2 water channelIntracellular vesiclesApical membrane proteinsMembrane-associated proteinsTrafficking of AQP2Apical surface expressionEpithelial cellsCell surface retentionApical plasma membraneInvolvement of MALBody water homeostasisS256 phosphorylationWater channel proteinsSurface expressionApical deliveryRegulated traffickingSorting eventsRenal epithelial cellsMembrane associationMembrane proteinsPosttranslational modificationsProtein interactionsPlasma membraneChannel proteinsWater channelsMembrane Topography of the Hydrophobic Anchor Sequence of Poliovirus 3A and 3AB Proteins and the Functional Effect of 3A/3AB Membrane Association upon RNA Replication †
Fujita K, Krishnakumar SS, Franco D, Paul AV, London E, Wimmer E. Membrane Topography of the Hydrophobic Anchor Sequence of Poliovirus 3A and 3AB Proteins and the Functional Effect of 3A/3AB Membrane Association upon RNA Replication †. Biochemistry 2007, 46: 5185-5199. PMID: 17417822, PMCID: PMC2519882, DOI: 10.1021/bi6024758.Peer-Reviewed Original ResearchConceptsModel membrane vesiclesAnchor sequenceHydrophobic anchor sequenceMembrane vesiclesViral protein 3ABFull-length proteinN-terminal boundaryTransmembrane topographyMembrane associationSuppressor mutationsTransmembrane segmentsProtein 3ABRNA polymeraseMembranous vesiclesC-terminusMembrane topographyCytoplasmic surfaceHost cellsRNA replicationPoliovirus RNAHeLa cellsSingle tryptophanProteinUridylylation reactionLipid bilayers
2006
Shigella IpgB1 promotes bacterial entry through the ELMO–Dock180 machinery
Handa Y, Suzuki M, Ohya K, Iwai H, Ishijima N, Koleske AJ, Fukui Y, Sasakawa C. Shigella IpgB1 promotes bacterial entry through the ELMO–Dock180 machinery. Nature Cell Biology 2006, 9: 121-128. PMID: 17173036, DOI: 10.1038/ncb1526.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsBacterial AdhesionCell LineCell MembraneDogsHeLa CellsHumansImmunoprecipitationMiceModels, BiologicalNIH 3T3 CellsProtein Transportrac GTP-Binding Proteinsrac1 GTP-Binding ProteinRNA InterferenceShigellaSignal TransductionTransduction, GeneticTransfectionConceptsMembrane rufflesCell motility proteinsRole of RhoGEpithelial cellsType III secretionWild-type cellsMembrane associationMotility proteinsPulldown assaysBinding partnerDock180 pathwayBacterial entryRufflesRac1 activityIpgB1EffectorsPivotal roleCellsELMODock180RhoGSpecial mechanismShigellaMachineryEngulfmentPrenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III Activity and Chitin Chain Length▿
Grabińska K, Magnelli P, Robbins P. Prenylation of Saccharomyces cerevisiae Chs4p Affects Chitin Synthase III Activity and Chitin Chain Length▿. MSphere 2006, 6: 328-336. PMID: 17142567, PMCID: PMC1797950, DOI: 10.1128/ec.00203-06.Peer-Reviewed Original ResearchConceptsChitin synthase IIIChitin synthase III activityPlasma membrane associationC-terminal endMembrane associationCSIII activityChs4pCatalytic subunitProtein factorsChitin biosynthesisSynthase IIIFarnesyl transferaseYeast cellsPrenylationChitin polymersPrenyl moietyEnzymatic activityChitin contentAttachment sitesAverage chain lengthChs3pSaccharomycesVivoBiosynthesisFTaseIn Vivo Dynamics of Rac-Membrane Interactions
Moissoglu K, Slepchenko BM, Meller N, Horwitz AF, Schwartz MA. In Vivo Dynamics of Rac-Membrane Interactions. Molecular Biology Of The Cell 2006, 17: 2770-2779. PMID: 16597700, PMCID: PMC1474787, DOI: 10.1091/mbc.e06-01-0005.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsCell MembraneComputer SimulationDiffusionGenes, ReporterGuanine Nucleotide Dissociation InhibitorsKineticsMiceMicroscopy, ConfocalModels, TheoreticalPlasmidsProtein Transportrac GTP-Binding ProteinsRecombinant Fusion ProteinsRecombinant Proteinsrho-Specific Guanine Nucleotide Dissociation InhibitorsConceptsGuanine Nucleotide Dissociation InhibitorGTPase-activating proteinsGTP-RacNucleotide exchange factorsVivo dynamicsSmall hairpin RNADissociation inhibitorMembrane associationExchange factorRac functionGEF Tiam1Hairpin RNARhoGDIPhotobleaching methodRacCytosolOverexpressionMajor routeDissociation rate constantsTiam1RNAProteinDetectable rateMembraneActivationPalmitoylation of the EGFR Ligand Spitz by Rasp Increases Spitz Activity by Restricting Its Diffusion
Miura GI, Buglino J, Alvarado D, Lemmon MA, Resh MD, Treisman JE. Palmitoylation of the EGFR Ligand Spitz by Rasp Increases Spitz Activity by Restricting Its Diffusion. Developmental Cell 2006, 10: 167-176. PMID: 16459296, DOI: 10.1016/j.devcel.2005.11.017.Peer-Reviewed Original ResearchMeSH KeywordsAcyltransferasesAnimalsBase SequenceBiological Transport, ActiveCell LineCell MembraneCysteineDNADrosophilaDrosophila ProteinsEpidermal Growth FactorErbB ReceptorsFemaleGenes, InsectIn Vitro TechniquesLigandsMaleMembrane ProteinsModels, BiologicalMutagenesis, Site-DirectedMutationOvaryPalmitic AcidRecombinant ProteinsTransfectionWings, AnimalConceptsEpidermal growth factor receptorDrosophila epidermal growth factor receptorEGFR ligand SpitzPlasma membrane associationN-terminal cysteine residueLigand SpitzMembrane associationWnt familyDevelopmental functionsGrowth factor receptorCysteine residuesBiological functionsLipid modificationPalmitoylationIntracellular proteinsCultured cellsCell membraneFactor receptorSpitzReduced activityVivoTransmembraneHedgehogProteinActivity
2003
Chapter 150 Pleckstrin Homology (PH) Domains
Lemmon M. Chapter 150 Pleckstrin Homology (PH) Domains. 2003, 161-169. DOI: 10.1016/b978-012124546-7/50511-8.Peer-Reviewed Original ResearchPleckstrin homology domainPH domainHomology domainSequence similarityPH domain-containing proteinsDomain-containing proteinsHuman genome sequenceMembrane traffickingConserved motifsMembrane associationCommon foldCellular signalingGenome sequenceCytoskeletal organizationDomain familySequence identityFunctional relatednessProtein ligandsHigh affinityProteinPhospholipid modificationStructural similarityPhosphoinositideSequenceDomain
2001
Caspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*
Lee A, Morrow J, Fowler V. Caspase Remodeling of the Spectrin Membrane Skeleton during Lens Development and Aging*. Journal Of Biological Chemistry 2001, 276: 20735-20742. PMID: 11278555, DOI: 10.1074/jbc.m009723200.Peer-Reviewed Original ResearchConceptsLens fiber cellsFiber cellsMembrane blebbingMembrane skeletonLens developmentAlpha-spectrinSpectrin membrane skeletonMembrane skeleton componentsChick lens developmentCell-cell fusionApoptotic cellsOldest fiber cellsMembrane associationClassical apoptosisApoptotic processSpecific proteolysisTerminal differentiationAdult lensSpectrin fragmentsMembrane interdigitationsBlebbingCytoskeletal protein alpha-spectrinPermanent remodelingSkeleton componentsSpectrin
2000
Signal-dependent membrane targeting by pleckstrin homology (PH) domains
LEMMON M, FERGUSON K. Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochemical Journal 2000, 350: 1-18. DOI: 10.1042/bj3500001.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsPleckstrin homology domainPH domainHomology domainSignal-dependent recruitmentSmall protein modulesDifferent protein ligandsMost PH domainsGreen fluorescent proteinMembrane associationProtein modulesCellular signalingDynamin 1Cytoskeletal rearrangementsCell signalingOligomeric statePlasma membraneMembrane bindingStructural basisHost proteinsFluorescent proteinProtein ligandsPhysiological functionsPhysiological roleAmino acidsPhosphoinositide
1999
Molecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*
Luan P, Balch W, Emr S, Burd C. Molecular Dissection of Guanine Nucleotide Dissociation Inhibitor Function in Vivo Rab-INDEPENDENT BINDING TO MEMBRANES AND ROLE OF RAB RECYCLING FACTORS*. Journal Of Biological Chemistry 1999, 274: 14806-14817. PMID: 10329679, DOI: 10.1074/jbc.274.21.14806.Peer-Reviewed Original ResearchConceptsRecycling factorNucleotide Dissociation InhibitorFusion of vesiclesSite-directed mutagenesisAmino acid residuesRab deliveryDistinct RabsRab GTPasesRab proteinsRab-GDPDissociation inhibitorMembrane associationEssential proteinsMolecular dissectionEndocytic pathwayGDI functionAcid residuesRabCellular membranesDominant inhibitionMultiple effectorsRate of recyclingInhibitor functionProteinEndogenous pool
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