2021
Phosphatidylserine binding directly regulates TIM-3 function
Smith CM, Li A, Krishnamurthy N, Lemmon MA. Phosphatidylserine binding directly regulates TIM-3 function. Biochemical Journal 2021, 478: 3331-3349. PMID: 34435619, PMCID: PMC8454703, DOI: 10.1042/bcj20210425.Peer-Reviewed Original ResearchConceptsTim-3T cell receptorTherapeutic targetCo-signaling receptorsTim-3 functionTim-3 ligandTim-3 signalingCo-inhibitory receptorsCo-stimulatory receptorsImmune modulation approachesIL-2 secretionPotential therapeutic targetNF-κB signalingImportant therapeutic targetPD-1Jurkat cellsCultured Jurkat cellsT cellsCell receptorTCR stimulationReceptorsImportance of phosphatidylserineDifferent studiesCellsSignaling
2018
Flipping ATP to AMPlify Kinase Functions
Sheetz JB, Lemmon MA. Flipping ATP to AMPlify Kinase Functions. Cell 2018, 175: 641-642. PMID: 30340038, PMCID: PMC6421561, DOI: 10.1016/j.cell.2018.10.011.Peer-Reviewed Original Research
2004
Svp1p defines a family of phosphatidylinositol 3,5‐bisphosphate effectors
Dove SK, Piper RC, McEwen RK, Yu JW, King MC, Hughes DC, Thuring J, Holmes AB, Cooke FT, Michell RH, Parker PJ, Lemmon MA. Svp1p defines a family of phosphatidylinositol 3,5‐bisphosphate effectors. The EMBO Journal 2004, 23: 1922-1933. PMID: 15103325, PMCID: PMC404323, DOI: 10.1038/sj.emboj.7600203.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutophagy-Related ProteinsBase SequenceCloning, MolecularEndosomesEscherichia coliGene ComponentsGenetic VectorsGreen Fluorescent ProteinsMembrane ProteinsMolecular Sequence DataPhosphatidylinositol PhosphatesPhosphotransferases (Alcohol Group Acceptor)PlasmidsProtein BindingProtein FoldingProtein TransportRhinovirusSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Analysis, DNAVacuolesConceptsFamily of phosphatidylinositolSaccharomyces cerevisiae mutantsDrosophila homologueCerevisiae mutantsMembrane recyclingVesicle recyclingVacuole enlargementVacuole membraneMultivesicular bodiesRelated proteinsLysosomal compartmentMarker proteinsExquisite specificityEffectorsProteinPhosphatidylinositolVacuolesEukaryotesCellsMutantsLocalisesGolgiHomologuesMVBGenes
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
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 mechanismRegulationPathwayCellsFunctionAdhesionSpecific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells
Artalejo C, Lemmon M, Schlessinger J, Palfrey H. Specific role for the PH domain of dynamin‐1 in the regulation of rapid endocytosis in adrenal chromaffin cells. The EMBO Journal 1997, 16: 1565-1574. PMID: 9130701, PMCID: PMC1169760, DOI: 10.1093/emboj/16.7.1565.Peer-Reviewed Original ResearchMeSH KeywordsAdrenal MedullaAmino Acid SequenceAnimalsBlood ProteinsCattleChromaffin CellsDynamin IDynaminsEndocytosisGenetic VariationGTP PhosphohydrolasesHumansModels, StructuralMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesPhosphoproteinsPolymerase Chain ReactionProtein Structure, SecondaryRecombinant ProteinsSequence Homology, Amino AcidConceptsPH domainDynamin 1Rapid endocytosisPleckstrin homology domainAmino acidsDynamin PH domainIsolated PH domainTypes of endocytosisChromaffin cellsHomology domainDynamin 2Mutational studiesEquivalent residuesEndocytotic processDifferent isoformsAdrenal chromaffin cellsEndocytosisDynaminVariable loopScission eventsSpecific roleCellsKey roleDomainIsoforms