2024
Ectopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation
Falahati H, Wu Y, Fang M, De Camilli P. Ectopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation. Current Biology 2024 PMID: 39626668, DOI: 10.1016/j.cub.2024.11.010.Peer-Reviewed Original ResearchEndoplasmic reticulumSpine apparatusActin bundlesEndomembrane networkER sheetsConserved regionProtein synaptopodinCisternal organelleNon-neuronal cellsER cisternsOrganellesSynaptopodinProteinNeuronal dendritesNeuronal spinesAxon initial segmentFindings shed lightBiogenesisActinProtein matrixNarrow lumenReticulumMammalsInitial segmentMechanism
2019
PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes
Guillén-Samander A, Bian X, De Camilli P. PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 22619-22623. PMID: 31636202, PMCID: PMC6842579, DOI: 10.1073/pnas.1913509116.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumLipid transportLate endosomes/lysosomesIntrinsic membrane proteinsLipid transport proteinsEndosomes/lysosomesEndocytic membranesDomain familyMembrane proteinsLate endosomesEndocytic flowMolecular inventoryTransport proteinsPDZD8ProteinLysosomesMembraneEndosomesAdjacent bilayersReticulum
2017
Contacts between the endoplasmic reticulum and other membranes in neurons
Wu Y, Whiteus C, Xu CS, Hayworth KJ, Weinberg RJ, Hess HF, De Camilli P. Contacts between the endoplasmic reticulum and other membranes in neurons. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: e4859-e4867. PMID: 28559323, PMCID: PMC5474793, DOI: 10.1073/pnas.1701078114.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumER–plasma membrane contactsER-PM contactsMembrane contactSmaller focal contactsRegulation of CaInterorganelle communicationOrganelle biogenesisDifferent neuronal compartmentsCell physiologyIntracellular membranesFocal contactsMultivesicular bodiesER contactsIntracellular organellesER cisternaeLipid homeostasisBiochemical studiesTubulovesicular structuresMembrane appositionNeuronal compartmentsImportant functionsMitochondriaReticulumMembraneLipid transport by TMEM24 at ER–plasma membrane contacts regulates pulsatile insulin secretion
Lees JA, Messa M, Sun EW, Wheeler H, Torta F, Wenk MR, De Camilli P, Reinisch KM. Lipid transport by TMEM24 at ER–plasma membrane contacts regulates pulsatile insulin secretion. Science 2017, 355 PMID: 28209843, PMCID: PMC5414417, DOI: 10.1126/science.aah6171.Peer-Reviewed Original ResearchConceptsER–plasma membrane contactsLipid transportLipid-binding modulesMembrane contactPhosphoinositide signalingMembrane proteinsPrecursor phosphatidylinositolProtein 24Reversible localizationEndoplasmic reticulumTMEM24Β-cellsPhosphatidylinositolInsulin secretionCalcium oscillationsCytosolic calciumDephosphorylationType II diabetesPhosphorylationSignalingProteinReticulumSecretionII diabetesTransport
2016
Endosome-ER Contacts Control Actin Nucleation and Retromer Function through VAP-Dependent Regulation of PI4P
Dong R, Saheki Y, Swarup S, Lucast L, Harper JW, De Camilli P. Endosome-ER Contacts Control Actin Nucleation and Retromer Function through VAP-Dependent Regulation of PI4P. Cell 2016, 166: 408-423. PMID: 27419871, PMCID: PMC4963242, DOI: 10.1016/j.cell.2016.06.037.Peer-Reviewed Original Research
2015
SMP-domain proteins at membrane contact sites: Structure and function
Reinisch KM, De Camilli P. SMP-domain proteins at membrane contact sites: Structure and function. Biochimica Et Biophysica Acta 2015, 1861: 924-927. PMID: 26686281, PMCID: PMC4902782, DOI: 10.1016/j.bbalip.2015.12.003.Peer-Reviewed Original ResearchConceptsMembrane contact sitesContact sitesAnant K. MenonCellular lipid landscapeTim P. LevineER-mitochondrial contactsSMP domainLipid landscapeComplex subunitsPlasma membraneMolecular basisLipid transportersEndoplasmic reticulumProteinRecent discoveryMembraneSuch sitesSitesSubunitsReticulumTransportersGlycerolipidsRegulationElucidationSpecial issue
1989
Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor
Mignery G, Südhof T, Takei K, De Camilli P. Putative receptor for inositol 1,4,5-trisphosphate similar to ryanodine receptor. Nature 1989, 342: 192-195. PMID: 2554146, DOI: 10.1038/342192a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium ChannelsCerebellumCloning, MolecularFluorescent Antibody TechniqueImmunohistochemistryInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsIntracellular MembranesMiceMolecular Sequence DataPurkinje CellsReceptors, Cell SurfaceReceptors, CholinergicReceptors, Cytoplasmic and NuclearRyanodineRyanodine Receptor Calcium Release ChannelConceptsEndoplasmic reticulumCalcium channel proteinsIntracellular second messengerRelative molecular massIntracellular membranesSecond messengerIntracellular compartmentsMolecular massEfficacy of neurotransmissionPutative receptorDirect roleProteinCalcium releaseGrowth factorReticulumDendritic spinesTrisphosphateIntracellular storesPresynaptic terminalsInositolIntracellular calcium storesReceptorsCalcium storesRNA6Immunocytochemistry