2022
In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts
Cai S, Wu Y, Guillén-Samander A, Hancock-Cerutti W, Liu J, De Camilli P. In situ architecture of the lipid transport protein VPS13C at ER–lysosome membrane contacts. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2203769119. PMID: 35858323, PMCID: PMC9303930, DOI: 10.1073/pnas.2203769119.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumCryo-focused ion beam millingMembrane contact sitesCryo-electron tomographyFull-length structureLipid transport proteinsRod-like densitiesLysosome contactBinding partnerGenetic approachesHydrophobic grooveTransport proteinsContact sitesVps13Lipid transportAlphaFold predictionsFull-length modelHeLa cellsMembrane contactSitu architectureAdjacent membranesVPS13CProteinStructural informationEndo/lysosomes
2009
Mechanistic Insights into Membrane Remodeling Through BAR‐Domain Proteins
Frost A, Mim C, Perera R, Spasov K, Egelman E, De Camilli P, Unger V. Mechanistic Insights into Membrane Remodeling Through BAR‐Domain Proteins. The FASEB Journal 2009, 23: 82.2-82.2. DOI: 10.1096/fasebj.23.1_supplement.82.2.Peer-Reviewed Original ResearchF-BAR domainBAR domain proteinsMembrane-bound stateDifferent molecular surfacesMembrane remodelingCellular physiologyMembrane curvatureElectron cryomicroscopyMechanistic insightsCooperative assemblyConstituent membranesProteinStructural informationMolecular surfaceFunctional stateMembraneDomainSubtle changesCryomicroscopyBilayer substratePhysiologyStructural modelAssemblyRemodelingCells