Shanta Nag
Research Associate Cell BiologyCards
About
Research
Publications
2026
Legionella Lem26 functions as an ATG8-activated effector that inhibits host autophagy
Parducho K, Yang Z, Guinn E, Choi D, Nag S, Melia T, Roy C. Legionella Lem26 functions as an ATG8-activated effector that inhibits host autophagy. MBio 2026, 17: e03595-25. PMID: 41641997, PMCID: PMC12977470, DOI: 10.1128/mbio.03595-25.Peer-Reviewed Original ResearchConceptsIntracellular pathogen Legionella pneumophila utiSaccharomyces cerevisiaeHost autophagy pathwayHost autophagyLegionella pneumophilaEffector proteinsProximity labelingADP-ribosyltransferaseAutophagy pathwayPosttranslational modificationsAutophagic membranesAutophagosomal membranesDot/Icm type IVB secretion systemProteolytic processingType IVB secretion systemPosttranslational modifications of proteinsIVB secretion systemMultiple effector proteinsATG8-interacting motifMammalian cell lysatesADP-ribosyltransferase activityModification of proteinsInnate immune pathwaysATG8 proteinsSecretion system
2025
SNARE Proteins Are Required for Macroautophagy
Nair U, Jotwani A, Geng J, Gammoh N, Richerson D, Yen W, Griffith J, Nag S, Wang K, Moss T, Baba M, McNew J, Jiang X, Reggiori F, Melia T, Klionsky D. SNARE Proteins Are Required for Macroautophagy. Cell 2025, 188: 6687. PMID: 41177156, PMCID: PMC12710386, DOI: 10.1016/j.cell.2025.10.018.Peer-Reviewed Original Research
2014
Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3
Nath S, Dancourt J, Shteyn V, Puente G, Fong WM, Nag S, Bewersdorf J, Yamamoto A, Antonny B, Melia TJ. Lipidation of the LC3/GABARAP family of autophagy proteins relies on a membrane-curvature-sensing domain in Atg3. Nature Cell Biology 2014, 16: 415-424. PMID: 24747438, PMCID: PMC4111135, DOI: 10.1038/ncb2940.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsApoptosis Regulatory ProteinsAutophagy-Related Protein 7Autophagy-Related Protein 8 FamilyAutophagy-Related ProteinsCell MembraneCytoskeletal ProteinsHeLa CellsHumansHydrophobic and Hydrophilic InteractionsLiposomesMembrane ProteinsMiceMice, KnockoutMicrofilament ProteinsMicrotubule-Associated ProteinsMutationPhosphatidylethanolaminesRatsSignal TransductionStress, PhysiologicalTransfectionUbiquitin-Activating EnzymesUbiquitin-Conjugating EnzymesConceptsLipid-packing defectsLC3/GABARAP familyLC3/GABARAP lipidationAmino-terminal amphipathic helixE2-like enzymeGABARAP familyAutophagic machineryIsolation membraneAmphipathic helixIntracellular membranesAutophagy proteinsRescue experimentsATG3LipidationCurved rimProteinMotifPhysiologic roleMembranePhagophoreAutophagosomesMachineryHelixEnzyme
2011
SNARE Proteins Are Required for Macroautophagy
Nair U, Jotwani A, Geng J, Gammoh N, Richerson D, Yen WL, Griffith J, Nag S, Wang K, Moss T, Baba M, McNew JA, Jiang X, Reggiori F, Melia TJ, Klionsky DJ. SNARE Proteins Are Required for Macroautophagy. Cell 2011, 146: 290-302. PMID: 21784249, PMCID: PMC3143362, DOI: 10.1016/j.cell.2011.06.022.Peer-Reviewed Original ResearchConceptsAutophagosome biogenesisAutophagosome membrane expansionV-SNAREs Sec22Vacuole/lysosomeDouble-membrane autophagosomesT-SNAREsAtg9 transportSNARE proteinsDe novo formationAutophagy componentsFusion eventsMembrane expansionTubulovesicular clustersNovo formationAtg8BiogenesisMacroautophagyProteinPhysiological concentrationsSec22Atg9Ykt6Tlg2OrganellesAutophagosomes
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