2014
Putting together structures of epidermal growth factor receptors
Bessman NJ, Freed DM, Lemmon MA. Putting together structures of epidermal growth factor receptors. Current Opinion In Structural Biology 2014, 29: 95-101. PMID: 25460273, PMCID: PMC4268130, DOI: 10.1016/j.sbi.2014.10.002.Peer-Reviewed Original ResearchConceptsEpidermal growth factor receptorGrowth factor receptorIntact epidermal growth factor receptorChemical biology methodsNumerous crystal structuresFactor receptorTyrosine kinase domainVariety of inhibitorsKinase domainExtracellular regionMembrane environmentIntracellular regionBiology methodsIntact receptorReceptorsCancer therapyNext challengeCrystal structureMembraneActivationRegionInhibitorsDomain
2009
Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae
Nishihama R, Schreiter JH, Onishi M, Vallen EA, Hanna J, Moravcevic K, Lippincott MF, Han H, Lemmon MA, Pringle JR, Bi E. Role of Inn1 and its interactions with Hof1 and Cyk3 in promoting cleavage furrow and septum formation in S. cerevisiae. Journal Of Cell Biology 2009, 185: 995-1012. PMID: 19528296, PMCID: PMC2711614, DOI: 10.1083/jcb.200903125.Peer-Reviewed Original ResearchConceptsCleavage furrowChitin synthase Chs2C-terminal regionActomyosin ring contractionCytokinesis proteinsDivision siteMitotic exitPXXP motifSH3 domainSeptum formationC2 domainS. cerevisiaePlasma membraneBind phospholipidsAMR contractionN-terminusCyk3Inn1Extracellular matrixChs2ProteinImportant interactionsHof1MembraneCytokinesis
2007
Investigation of Novel Molecular Targets for Pleckstrin Homology (PH) Domains Found in Oncogenes Implicated in Breast Cancer
Keleti D, Lemmon M. Investigation of Novel Molecular Targets for Pleckstrin Homology (PH) Domains Found in Oncogenes Implicated in Breast Cancer. 2007 DOI: 10.21236/ada469536.Peer-Reviewed Original ResearchHomology domainPH domainHuman PH domainsOSBP PH domainHost adaptor proteinsMembrane-targeting modulesPleckstrin homology domainGTPase Arf1Adaptor proteinNovel molecular targetsS. cerevisiaePlasma membraneMembrane lipidsSpecific membraneHigh affinityPPInsDirect interactionComparable affinityDomain classesMolecular targetsGolgiBinding propertiesMembraneRecent studiesAffinity
2001
High-Affinity Binding of a FYVE Domain to Phosphatidylinositol 3-Phosphate Requires Intact Phospholipid but Not FYVE Domain Oligomerization †
Sankaran V, Klein D, Sachdeva M, Lemmon M. High-Affinity Binding of a FYVE Domain to Phosphatidylinositol 3-Phosphate Requires Intact Phospholipid but Not FYVE Domain Oligomerization †. Biochemistry 2001, 40: 8581-8587. PMID: 11456498, DOI: 10.1021/bi010425d.Peer-Reviewed Original ResearchMeSH KeywordsBinding, CompetitiveBlood ProteinsCarrier ProteinsCation Transport ProteinsGlutathione TransferaseGuanine Nucleotide Exchange FactorsHeLa CellsHumansLiposomesMonosaccharide Transport ProteinsPhosphatidylinositol PhosphatesPhospholipidsPhosphoproteinsProtein BindingProtein Structure, TertiaryProteinsRecombinant Fusion ProteinsSymportersZinc FingersConceptsFYVE domainPH domainDomain oligomerizationSpecific PH domainsVacuolar protein sortingPleckstrin homology domainLipid headgroupsProtein sortingMembrane trafficHomology domainSpecific phosphoinositideLike domainEndosomal maturationHigh-affinity bindingPreferred lipidPhospholipase CPhosphoinositideIntact lipidsIntact phospholipidsOligomerizationDomainMembrane
1999
Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain
Lee A, Frank D, Marks M, Lemmon M. Dominant-negative inhibition of receptor-mediated endocytosis by a dynamin-1 mutant with a defective pleckstrin homology domain. Current Biology 1999, 9: 261-265. PMID: 10074457, DOI: 10.1016/s0960-9822(99)80115-8.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainReceptor-mediated endocytosisDynamin 1Homology domainEndocytic vesiclesPH domain bindsDynamin PH domainDominant negative inhibitorHigher-order oligomersDominant-negative inhibitionDynamin functionDomain bindsDynamin oligomersGTP bindingGTP hydrolysisGTPase activityPlasma membraneDynaminEndocytosisVesiclesPhosphoinositideBindsDomainMembrane
1997
Regulatory recruitment of signalling molecules to the cell membrane by pleckstrinhomology domains
M.A. L, M. F, J. S, K. F. Regulatory recruitment of signalling molecules to the cell membrane by pleckstrinhomology domains. Trends In Cell Biology 1997, 7: 237-242. PMID: 17708952, DOI: 10.1016/s0962-8924(97)01065-9.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsCell membraneSmall protein modulesPleckstrin homology domainPH domainProtein modulesBiological functionsDiverse processesCertain proteinsSpecific membraneProtein synthesisCell adhesionDNA synthesisProteinMembraneRecent studiesRecruitmentDomainPhosphoinositideEfficient mechanismRegulationPathwayCellsFunctionAdhesion
1993
Simulation of helix association in membranes: modeling the glycophorin A transmembrane domain
Treutlein H, Lemmon M, Engleman D, Brunger A. Simulation of helix association in membranes: modeling the glycophorin A transmembrane domain. 1993, i: 708-714 vol.1. DOI: 10.1109/hicss.1993.270670.Peer-Reviewed Original ResearchDimeric membrane proteinAmino acid sequenceRight-handed supercoilTransmembrane domainTransmembrane structureMembrane proteinsTransmembrane regionHelical proteinsMutagenesis dataHelix associationSecondary structureGlycophorin ALipid bilayersHelical dimerProteinStructural informationHelixConformationLocal energy minimaMembraneMolecular dynamics simulationsSupercoilsMutagenesisEnergy minimaInteraction energy