2024
Methylarginine targeting chimeras for lysosomal degradation of intracellular proteins
Seabrook L, Franco C, Loy C, Osman J, Fredlender C, Zimak J, Campos M, Nguyen S, Watson R, Levine S, Khalil M, Sumigray K, Trader D, Albrecht L. Methylarginine targeting chimeras for lysosomal degradation of intracellular proteins. Nature Chemical Biology 2024, 20: 1566-1576. PMID: 39414979, DOI: 10.1038/s41589-024-01741-y.Peer-Reviewed Original ResearchProtein arginine methyltransferasesTarget proteinsLoss-of-function phenotypesDegradation of intracellular proteinsUbiquitin-proteasome pathwayHistone deacetylase 6Bromodomain-containing protein 4Discovery of small moleculesTargeted Protein DegradationDegrade target proteinsTargeting chimerasArginine methylationArginine methyltransferasesProtein methylationPathogenic proteinsLysosomal deliveryLysosomal pathwayIntracellular proteinsLysosomal degradationHeterobifunctional small moleculesProtein degradationSmall-molecule degradersLysosomal proteolysisSubstrate degradationSmall molecules
2023
LC3B is lipidated to large lipid droplets during prolonged starvation for noncanonical autophagy
Omrane M, Ben M'Barek K, Santinho A, Nguyen N, Nag S, Melia T, Thiam A. LC3B is lipidated to large lipid droplets during prolonged starvation for noncanonical autophagy. Developmental Cell 2023, 58: 1266-1281.e7. PMID: 37315562, PMCID: PMC10686041, DOI: 10.1016/j.devcel.2023.05.009.Peer-Reviewed Original ResearchConceptsProtein 1 light chain 3BLarge lipid dropletsLight chain 3BStarvation triggersLipidation reactionNoncanonical autophagyLysosomal pathwayAutophagic processStore lipidsAutophagy mechanismLipid dropletsATG3Large LDsProlonged starvationHuman liver cellsLC3BTimes of scarcityStarvationLiver cellsMacrolipophagyAutophagicClose proximityAutophagyATG5MicrotubulesCoronaviruses, Lysosomes, and Secondary Bacterial Infections: Coronaviruses Outsmart the Host
Peng X, Dela Cruz C, Sharma L. Coronaviruses, Lysosomes, and Secondary Bacterial Infections: Coronaviruses Outsmart the Host. DNA And Cell Biology 2023, 42: 189-193. PMID: 36763591, DOI: 10.1089/dna.2023.0002.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsSecondary bacterial infectionCellular homeostatic functionsHomeostatic functionsExtensive cell deathBacterial infectionsLysosomal lumenLysosomal machineryKey organellesLysosomal pathwayUnique adaptationsExit cellsSevere acute respiratory syndrome coronavirus 2Cell deathCellular componentsAcute respiratory syndrome coronavirus 2Respiratory syndrome coronavirus 2Syndrome coronavirus 2Pathogen killingCoronavirus disease 2019LysosomesLysosomal enzymesLysosomal environmentCoronavirus 2Host immunityCausative agent
2021
Microglia regulate brain Progranulin levels through the endocytosis-lysosomal pathway
Dong T, Tejwani L, Jung Y, Kokubu H, Luttik K, Driessen TM, Lim J. Microglia regulate brain Progranulin levels through the endocytosis-lysosomal pathway. JCI Insight 2021, 6: e136147. PMID: 34618685, PMCID: PMC8663778, DOI: 10.1172/jci.insight.136147.Peer-Reviewed Original ResearchConceptsPGRN levelsNovel potential therapeutic targetFrontotemporal lobar degenerationPotential therapeutic targetNeuronal ceroid lipofuscinosisPGRN deficiencyPGRN expressionLysosomal pathwayProgranulin levelsPathological changesHaploinsufficient miceTherapeutic targetMicrogliaNeuropathological phenotypeAlzheimer's diseaseProgranulinCeroid lipofuscinosisGlycoprotein progranulinNeurodegenerative diseasesDiseaseMiceGenetic alterationsNemo-like kinaseGenetic interaction studiesGenetic variantsProtein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration
Nakamura T, Oh C, Zhang X, Lipton S. Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration. Free Radical Biology And Medicine 2021, 172: 562-577. PMID: 34224817, PMCID: PMC8579830, DOI: 10.1016/j.freeradbiomed.2021.07.002.Peer-Reviewed Original ResearchConceptsProtein misfoldingUbiquitin-proteasome systemCellular protein quality control machineryReactive oxygen speciesS-nitrosylationProtein quality control machineryQuality control machineryPost-translational modificationsNeurodegenerative diseasesProtein S-nitrosylationGenetic mutationsMost neurodegenerative diseasesMolecular chaperonesROS/RNSControl machineryLysosomal pathwayRare genetic mutationsMolecular mechanismsMolecular eventsMisfoldingMitochondrial dysfunctionTyrosine nitrationProteinOxygen speciesNeuronal demiseNEDD4 regulates ubiquitination and stability of the cell adhesion molecule IGPR-1 via lysosomal pathway
Sun L, Amraei R, Rahimi N. NEDD4 regulates ubiquitination and stability of the cell adhesion molecule IGPR-1 via lysosomal pathway. Journal Of Biomedical Science 2021, 28: 35. PMID: 33962630, PMCID: PMC8103646, DOI: 10.1186/s12929-021-00731-9.Peer-Reviewed Original ResearchConceptsCell adhesion molecule IGPR-1IGPR-1Lysosomal-dependent degradationUbiquitin E3Vivo co-immunoprecipitation assaysWild-type Nedd4Knockdown of NEDD4Polyproline-rich motifCritical cellular processesCell-cell adhesionCo-immunoprecipitation assaysTreatment of cellsCell surface levelsHEK-293 cellsA375 melanoma cellsWW domainsCellular processesRich motifLysosomal pathwayC-terminusNedd4Key regulatorLysosomal inhibitorsMolecular mechanismsMelanoma cell lines
2019
Neurofilament-lysosomal genetic intersections in the cortical network of stuttering
Benito-Aragón C, Gonzalez-Sarmiento R, Liddell T, Diez I, d'Oleire Uquillas F, Ortiz-Terán L, Bueichekú E, Chow H, Chang S, Sepulcre J. Neurofilament-lysosomal genetic intersections in the cortical network of stuttering. Progress In Neurobiology 2019, 184: 101718. PMID: 31669185, PMCID: PMC6938554, DOI: 10.1016/j.pneurobio.2019.101718.Peer-Reviewed Original ResearchConceptsCytoskeleton organizationNeurofilament genesCortical networksGenetic expression levelsMannose-6-phosphateGenetic interactomesInteractome networkTranscriptome dataLarge-scale cortical networksLysosomal pathwayAllen Human Brain AtlasPresence of stutteringGenetic intersectionFunctional connectivity MRIBiological functionsNeuronal circuitsSpatial similarity analysisGenesHuman Brain AtlasTarget pathwaysFunctional linkInteractomeNeurobiological underpinningsCo-localizationLysosomal dysfunction
1995
In vitro modeling of liver membrane copper transport
Schilsky M. In vitro modeling of liver membrane copper transport. Hepatology 1995, 22: 1340-1342. PMID: 7557893, DOI: 10.1002/hep.1840220449.Peer-Reviewed Original ResearchConceptsPlasma membrane vesiclesMembrane vesiclesCu transportGlutathione-conjugate transporterCanalicular plasma membrane vesiclesP-type ATPaseBasolateral plasma membrane vesiclesATPase inhibitor vanadatePlasma membrane fractionPresence of ATPAbsence of ATPVesicle transportRat liver plasma membrane vesiclesMammalian systemsP-type ATPase inhibitor vanadateLysosomal pathwayCu secretionLiver plasma membrane vesiclesATP-regenerating systemCu uptakeCopper transportRecent cloningMembrane fractionBiochemical evidenceVesicles
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