2022
SHIP164 is a chorein motif lipid transfer protein that controls endosome–Golgi membrane traffic
Hanna MG, Suen PH, Wu Y, Reinisch KM, De Camilli P. SHIP164 is a chorein motif lipid transfer protein that controls endosome–Golgi membrane traffic. Journal Of Cell Biology 2022, 221: e202111018. PMID: 35499567, PMCID: PMC9067936, DOI: 10.1083/jcb.202111018.Peer-Reviewed Original ResearchMeSH KeywordsCarrier ProteinsEndosomesGolgi ApparatusIntracellular MembranesIntracellular Signaling Peptides and ProteinsLipidsConceptsMannose-6-phosphate receptorCation-independent mannose-6-phosphate receptorMembrane contact sitesEarly endocytic pathwayGolgi membrane trafficLipid transfer proteinLipid transfer propertiesProtein-lipid ratioMembrane cargoMembrane trafficEndocytic membranesVesicular trafficRetrograde trafficEndocytic pathwayFunctional characterizationContact sitesMembranous organellesGolgi complexVesicle clustersCellular membranesTransfer proteinProteinLipid compositionOrganellesMembrane
2015
The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane
Baskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. Nature Cell Biology 2015, 18: 132-138. PMID: 26571211, PMCID: PMC4689616, DOI: 10.1038/ncb3271.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMutationPhosphatidylinositol PhosphatesProtein Structure, TertiaryProtein Transport
1999
The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*
Rosenthal J, Chen H, Slepnev V, Pellegrini L, Salcini A, Di Fiore P, De Camilli P. The Epsins Define a Family of Proteins That Interact with Components of the Clathrin Coat and Contain a New Protein Module*. Journal Of Biological Chemistry 1999, 274: 33959-33965. PMID: 10567358, DOI: 10.1074/jbc.274.48.33959.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid SequenceAnimalsCalcium-Binding ProteinsCarrier ProteinsCHO CellsClathrinCoated VesiclesCricetinaeDNA, ComplementaryFluorescent Antibody TechniqueGene ExpressionHumansIntracellular Signaling Peptides and ProteinsLuciferasesMaleMembrane ProteinsMolecular Sequence DataNeuropeptidesPhosphoproteinsPhylogenyProtein BindingProtein Structure, TertiaryRatsRecombinant Fusion ProteinsSequence AlignmentSequence Analysis, DNASequence Homology, Amino AcidTissue DistributionVesicular Transport ProteinsConceptsEpsin 1Clathrin coatClathrin adaptor AP-2New protein modulesNew protein familyTerminal regionAdaptor AP-2Family of proteinsRat brain libraryNPF motifsProtein modulesProtein familyCell peripheryAP-2Membrane dynamicsSimilar proteinsBrain libraryClathrinEps15Vesicle fractionEpsinGreen fluorescentGolgi regionCell surfaceProteinEpidermal growth factor pathway substrate 15, Eps15
Salcini A, Chen H, Iannolo G, De Camilli P, Di Fiore P. Epidermal growth factor pathway substrate 15, Eps15. The International Journal Of Biochemistry & Cell Biology 1999, 31: 805-809. PMID: 10481267, DOI: 10.1016/s1357-2725(99)00042-4.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsCalcium-Binding ProteinsCarrier ProteinsCell LineChromosomes, Human, Pair 1EndocytosisEpidermal Growth FactorHumansIntracellular Signaling Peptides and ProteinsNeuropeptidesPhosphoproteinsSignal TransductionTransferrinVesicular Transport ProteinsConceptsEpidermal growth factor receptorPutative coiled-coil regionCoiled-coil regionCell proliferationNIH 3T3 cellsReceptor-mediated endocytosisEH domainNH2-terminal portionEndocytic machineryEpsin functionIntracellular sortingEps15Growth factor receptorTerminal domainAP-2Kinase activityBinding proteinMultiple copiesBiomolecular strategiesProteinFactor receptorTripartite structureMLL geneGenesProliferationThe Interaction of Epsin and Eps15 with the Clathrin Adaptor AP-2 Is Inhibited by Mitotic Phosphorylation and Enhanced by Stimulation-dependent Dephosphorylation in Nerve Terminals*
Chen H, Slepnev V, Di Fiore P, De Camilli P. The Interaction of Epsin and Eps15 with the Clathrin Adaptor AP-2 Is Inhibited by Mitotic Phosphorylation and Enhanced by Stimulation-dependent Dephosphorylation in Nerve Terminals*. Journal Of Biological Chemistry 1999, 274: 3257-3260. PMID: 9920862, DOI: 10.1074/jbc.274.6.3257.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAnimalsBase SequenceCalcium-Binding ProteinsCarrier ProteinsCell LineDNA PrimersEndocytosisExocytosisIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMitosisNerve EndingsNeuropeptidesPhosphoproteinsPhosphorylationProtein BindingRatsVesicular Transport Proteins
1997
Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15
Haffner C, Takei K, Chen H, Ringstad N, Hudson A, Butler M, Salcini A, Di Fiore P, De Camilli P. Synaptojanin 1: localization on coated endocytic intermediates in nerve terminals and interaction of its 170 kDa isoform with Eps15. FEBS Letters 1997, 419: 175-180. PMID: 9428629, DOI: 10.1016/s0014-5793(97)01451-8.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCalcium-Binding ProteinsClathrinEndocytosisHumansImmunohistochemistryIntracellular Signaling Peptides and ProteinsMolecular Sequence DataNerve EndingsNerve Tissue ProteinsPhosphoproteinsPhosphoric Monoester HydrolasesRatsSequence AlignmentSynaptic TransmissionSynaptic VesiclesConceptsSynaptojanin 1Endocytic intermediatesClathrin-coated pitsCOOH-terminal regionEH domainSpecies threeEps15Multiplicity of interactionsPutative roleClathrinNerve terminalsEndocytosisIsoformsProteinPrevious dataMotifInositolIntermediatesBindingInteractionPhenylalanineLocalizationNew evidenceDomain
1988
[17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins
Lohmann S, De Camilli P, Walter U. [17] Type II cAMP-dependent protein kinase regulatory subunit-binding proteins. Methods In Enzymology 1988, 159: 183-193. PMID: 2842584, DOI: 10.1016/0076-6879(88)59019-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCarrier ProteinsCattleChromatography, DEAE-CelluloseCyclic AMPIntracellular Signaling Peptides and ProteinsKineticsMolecular WeightMyocardiumProtein BindingProtein KinasesConceptsRII subunitsCytosolic cAMP-dependent protein kinaseAdditional proteinsType II cAMP-dependent proteinCAMP-dependent protein kinaseCAMP-dependent proteinMicrotubule-associated proteinsRII overlayProtein kinaseSDS-polyacrylamide gel electrophoresisCertain proteinsNative stateProteinSteps of purificationGel electrophoresisSubunitsCellular structureAssay conditionsNonspecific interactionsRIIHigh affinityHigh enough affinityLight microscopyKinaseAffinity
1986
Interaction of the Regulatory Subunit (RII) of cAMP‐Dependent Protein Kinase with Tissue‐Specific Binding Proteins Including Microtubule‐Associated Proteinsa
LOHMANN S, WALTER U, DeCAMILLI P. Interaction of the Regulatory Subunit (RII) of cAMP‐Dependent Protein Kinase with Tissue‐Specific Binding Proteins Including Microtubule‐Associated Proteinsa. Annals Of The New York Academy Of Sciences 1986, 466: 449-452. PMID: 3460424, DOI: 10.1111/j.1749-6632.1986.tb38421.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainBrain ChemistryCarrier ProteinsCattleIntracellular Signaling Peptides and ProteinsMacromolecular SubstancesMicrotubule-Associated ProteinsMolecular WeightProtein Kinases