Peng Xu
Associate Research Scientist in NeuroscienceCards
About
Research
Publications
2025
Impaired hematopoiesis and embryonic lethality at midgestation of mice lacking both lipid transfer proteins VPS13A and VPS13C
Xu P, Mancuso R, Leonzino M, Zeiss C, Krause D, De Camilli P. Impaired hematopoiesis and embryonic lethality at midgestation of mice lacking both lipid transfer proteins VPS13A and VPS13C. PLOS Biology 2025, 23: e3003393. PMID: 40956846, PMCID: PMC12463328, DOI: 10.1371/journal.pbio.3003393.Peer-Reviewed Original ResearchConceptsInterferon-stimulated genesInnate immunityMembrane contact sitesEmbryonic developmentActivation of innate immunityFamily of proteinsMembranes of intracellular organellesLipid transport proteinsLoss of function mutationsAge-dependent neurodegenerative diseasesMammalian genomesGene duplicationSubcellular localizationVPS13 genesContact sitesEmbryonic lethalityRIG-ILipid transferIntracellular organellesFunction mutationsVPS13ALipid fluxUpregulation of interferon-stimulated genesTransport proteinsStimulated genesMultiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics
Dai A, Xu P, Amos C, Fujise K, Wu Y, Yang H, Eisen J, Guillén-Samander A, De Camilli P. Multiple interactions recruit BLTP2 to ER-PM contacts to control plasma membrane dynamics. Journal Of Cell Biology 2025, 224: e202504027. PMID: 40899996, PMCID: PMC12406788, DOI: 10.1083/jcb.202504027.Peer-Reviewed Original ResearchConceptsPlasma membraneTubular endosomesN-BAR domain proteinsER-PM contactsPlasma membrane dynamicsLipid transport functionLipid transfer proteinsDomain proteinsMembrane dynamicsN-BARLipid transportTransfer proteinCell typesEndosomesIntracellular vacuolesProteinTransport functionPM dynamicsMacropinosomesAdaptorMultiple interactionsLipidPhosphoinositideERVacuolesThe bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage
Wang X, Xu P, Bentley-DeSousa A, Hancock-Cerutti W, Cai S, Johnson B, Tonelli F, Shao L, Talaia G, Alessi D, Ferguson S, De Camilli P. The bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage. Nature Cell Biology 2025, 27: 776-789. PMID: 40211074, PMCID: PMC12081312, DOI: 10.1038/s41556-025-01653-6.Peer-Reviewed Original ResearchConceptsDisease genesResponse to lysosomal damageSurface of lysosomesER–lysosome contactsParkinson's disease genesDelivery to lysosomesLipid transport proteinsLysosomal damageVPS13 proteinsLysosomal surfaceDisease proteinsGenetic studiesDamaged lysosomesVPS13CLysosomal stressLipid transportLysosomesInhibited stateMembrane perturbationRab7Lysosomal dysfunctionProteinVps13LipidGenesBPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN
Amos C, Fujise K, Ugur B, Hanna M, Xu P, De Camilli P. BPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN. Biophysical Journal 2025, 124: 274a-275a. DOI: 10.1016/j.bpj.2024.11.1556.Peer-Reviewed Original ResearchBPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN
Amos C, Fujise K, Ugur B, Hanna M, Xu P, De Camilli P. BPS2025 - A role for the bridge-like lipid transfer protein VPS13D in the control of membrane dynamics at the trans Golgi/TGN. Biophysical Journal 2025, 124: 358a. DOI: 10.1016/j.bpj.2024.11.1947.Peer-Reviewed Original Research
2024
Parkinsonism Sac domain mutation in Synaptojanin-1 affects ciliary properties in iPSC-derived dopaminergic neurons
Rafiq N, Fujise K, Rosenfeld M, Xu P, De Camilli P. Parkinsonism Sac domain mutation in Synaptojanin-1 affects ciliary properties in iPSC-derived dopaminergic neurons. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2318943121. PMID: 38635628, PMCID: PMC11047088, DOI: 10.1073/pnas.2318943121.Peer-Reviewed Original ResearchConceptsSynaptojanin 1Endocytic factorsDA neuronsCilia-mediated signalingNerve terminalsIPSC-derived dopaminergic neuronsUbiquitin chainsUbiquitinated proteinsCiliary baseCilia lengthNeurological defectsDopaminergic neuronsProtein dynamicsDomain mutationsAssembly stateIsogenic controlsNeuronsAbnormal accumulationMutationsMiceFocal concentrationParkinsonPI(4UbiquitinEndocytosis
2023
Erythroid Differentiation Dependent Interaction of VPS13A with XK at the Plasma Membrane of K562 Cells
Amos C, Xu P, De Camilli P. Erythroid Differentiation Dependent Interaction of VPS13A with XK at the Plasma Membrane of K562 Cells. Contact 2023, 6: 25152564231215133. PMID: 38144430, PMCID: PMC10748539, DOI: 10.1177/25152564231215133.Peer-Reviewed Original Research
2022
ER-lysosome lipid transfer protein VPS13C/PARK23 prevents aberrant mtDNA-dependent STING signaling
Hancock-Cerutti W, Wu Z, Xu P, Yadavalli N, Leonzino M, Tharkeshwar AK, Ferguson SM, Shadel GS, De Camilli P. ER-lysosome lipid transfer protein VPS13C/PARK23 prevents aberrant mtDNA-dependent STING signaling. Journal Of Cell Biology 2022, 221: e202106046. PMID: 35657605, PMCID: PMC9170524, DOI: 10.1083/jcb.202106046.Peer-Reviewed Original ResearchConceptsParkinson's diseasePD pathogenesisLeucine-rich repeat kinase 2 (LRRK2) G2019S mutationCGAS-STING pathwayAccumulation of lysosomesDNA-sensing cGAS-STING pathwayImmune activationLipid profileSTING signalingG2019S mutationAutosomal recessive Parkinson's diseaseRecessive Parkinson's diseaseModel human cell linesHuman cell linesCell linesPathogenesisLate endosomes/lysosomesDiseaseVPS13CEndosomes/lysosomesCurrent studyTransfer proteinActivationCellsPathwayModulation of amyloid precursor protein cleavage by γ-secretase activating protein through phase separation
Jin C, Wang J, Wang Y, Jia B, Guo X, Yang G, Xu P, Greengard P, Zhou R, Shi Y. Modulation of amyloid precursor protein cleavage by γ-secretase activating protein through phase separation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2122292119. PMID: 35298330, PMCID: PMC8944281, DOI: 10.1073/pnas.2122292119.Peer-Reviewed Original ResearchConceptsAberrant cleavage of amyloid precursor proteinAssociated with Alzheimer's diseaseAPP-C99Cleavage of amyloid precursor proteinAmyloid precursor protein cleavageAmyloid precursor proteinPhase separation in vitroC-terminal fragmentDevelopment of potential therapeuticsSequence elementsPrecursor proteinAberrant cleavageProtein cleavageSubstrate sequestrationAlzheimer's diseaseGSAPProteinCleavagePotential therapeuticsC99SequenceAb42Increasing concentrationsCells
2021
GSAP regulates lipid homeostasis and mitochondrial function associated with Alzheimer’s disease
Xu P, Chang JC, Zhou X, Wang W, Bamkole M, Wong E, Bettayeb K, Jiang LL, Huang T, Luo W, Xu H, Nairn AC, Flajolet M, Ip NY, Li YM, Greengard P. GSAP regulates lipid homeostasis and mitochondrial function associated with Alzheimer’s disease. Journal Of Experimental Medicine 2021, 218: e20202446. PMID: 34156424, PMCID: PMC8222926, DOI: 10.1084/jem.20202446.Peer-Reviewed Original ResearchMeSH KeywordsAgingAlzheimer DiseaseAmyloid beta-Protein PrecursorAnimalsBase SequenceDisease Models, AnimalHippocampusHomeostasisHumansLipid MetabolismMice, Inbred C57BLMice, KnockoutMitochondriaMitochondrial MembranesModels, BiologicalNerve Tissue ProteinsNeuronsNuclear ProteinsOpen Field TestPhosphorylationProtein BindingProtein TransportProteinsTranscription, GeneticConceptsMitochondrial functionLipid homeostasisFe65-APP complexSingle-nuclei RNAseqBrain transcript levelsImpairs mitochondrial functionHuman genetic dataMAM localizationMultiple biological pathwaysImproved mitochondrial functionUnbiased proteomicsProtein phosphorylationSingle nucleotide polymorphismsTranscript levelsGenetic dataLipid environmentModulatory proteinsBiological pathwaysGSAP expressionGSAPLipid metabolismAlzheimer's diseaseHomeostasisAmyloidogenic processingAD pathogenesis
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