Philip Mannino
Research
Publications
2022
Quality control mechanisms that protect nuclear envelope identity and function
Mannino PJ, Lusk CP. Quality control mechanisms that protect nuclear envelope identity and function. Journal Of Cell Biology 2022, 221: e202205123. PMID: 36036741, PMCID: PMC9442147, DOI: 10.1083/jcb.202205123.Peer-Reviewed Original ResearchConceptsNuclear pore complexQuality control mechanismsNuclear envelopeCellular degradative machineryNE integrityGenome stabilityPore complexMembrane remodelingDegradative machineryOuter membraneDistinct biochemistryBiochemical identityEndoplasmic reticulumAutophagy mechanismControl mechanismsSelective barrierPore membraneMembraneRecent workEukaryotesProteomeDeleterious effectsSpecializationMechanismMachinery
2021
Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome
Chandra S, Mannino PJ, Thaller DJ, Ader NR, King MC, Melia TJ, Lusk CP. Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome. Journal Of Cell Biology 2021, 220: e202103030. PMID: 34714326, PMCID: PMC8575018, DOI: 10.1083/jcb.202103030.Peer-Reviewed Original ResearchMeSH KeywordsAutophagosomesAutophagyAutophagy-Related ProteinsCytoplasmic VesiclesGreen Fluorescent ProteinsNuclear EnvelopeProtein DomainsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipTime FactorsVacuolesVesicular Transport ProteinsConceptsInner nuclear membraneNuclear envelope lumenOuter nuclear membraneNuclear membraneSplit-GFP reporterNuclear envelope localizationINM proteinsAutophagy apparatusEnvelope localizationLumenal vesiclesLumenal domainCargo adaptorsAtg39Sequence elementsCorrelative lightVesiclesAutophagosomesMembraneNucleophagyAdaptorReporterProteinOverexpressionMotifNuclear detox of unsaturated fat
Mannino PJ, Lusk CP. Nuclear detox of unsaturated fat. Developmental Cell 2021, 56: 2539-2541. PMID: 34582769, DOI: 10.1016/j.devcel.2021.09.002.Peer-Reviewed Original ResearchDirect binding of ESCRT protein Chm7 to phosphatidic acid–rich membranes at nuclear envelope herniations
Thaller DJ, Tong D, Marklew CJ, Ader NR, Mannino PJ, Borah S, King MC, Ciani B, Lusk CP. Direct binding of ESCRT protein Chm7 to phosphatidic acid–rich membranes at nuclear envelope herniations. Journal Of Cell Biology 2021, 220: e202004222. PMID: 33464310, PMCID: PMC7816628, DOI: 10.1083/jcb.202004222.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid SequenceConserved SequenceEndosomal Sorting Complexes Required for TransportHydrophobic and Hydrophilic InteractionsLipid BilayersModels, BiologicalNuclear EnvelopeNuclear PorePhosphatidic AcidsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsNuclear pore complex biogenesisNuclear membrane remodelingNuclear envelope herniationsLAP2-emerinNE remodelingNPC assemblyComplex biogenesisHydrophobic stretchMembrane remodelingChm7Nuclear envelopePA bindingPA metabolismFunctional importanceDirect bindingAmino acidsPhosphatidic acidMembraneBindingHeh1RecruitmentESCRTBiogenesisRemodelingYeast