2024
Identification of polycystin 2 missense mutants targeted for endoplasmic reticulum-associated degradation
Guerriero C, Carattino M, Sharp K, Kantz L, Gresko N, Caplan M, Brodsky J. Identification of polycystin 2 missense mutants targeted for endoplasmic reticulum-associated degradation. American Journal Of Physiology - Cell Physiology 2024, 328: c483-c499. PMID: 39714991, PMCID: PMC12168846, DOI: 10.1152/ajpcell.00776.2024.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulum-associated degradationPolycystin-2Autosomal dominant polycystic kidney diseaseEndoplasmic reticulum-associated degradation pathwayMissense mutationsGrowth of yeast strainsDisease-causing missense mutationsDisease-associated mutantsProteasome-dependent degradationHEK293 cellsConsistent with defectsDisease-linked mutationsHEK293 cell modelYeast modelYeast systemYeast strainsGenetic systemTreat autosomal dominant polycystic kidney diseaseMissense variantsProtein misfoldingProtein foldingCellular processesIncreased polyubiquitinationMisfolding phenotypeChemical chaperonesEnhanced eMAGE applied to identify genetic factors of nuclear hormone receptor dysfunction via combinatorial gene editing
Ciaccia P, Liang Z, Schweitzer A, Metzner E, Isaacs F. Enhanced eMAGE applied to identify genetic factors of nuclear hormone receptor dysfunction via combinatorial gene editing. Nature Communications 2024, 15: 5218. PMID: 38890276, PMCID: PMC11189492, DOI: 10.1038/s41467-024-49365-z.Peer-Reviewed Original ResearchConceptsGenome modificationEngineered nucleasesMultiplex genome engineeringEfficient multiplex editingLigand-binding domain of human estrogen receptor alphaMethods of genome editingCancer-associated mutationsHomology-directed repairMismatch repair systemLigand-binding domainSaccharomyces cerevisiaeYeast modelSynthetic genomesGenome engineeringPolygenic basisComplex phenotypesBackground mutationsGenomeGenome editingMultiplex editingEditing frequencyHuman estrogen receptor alphaDNA breaksEstrogen receptor alphaMMR inactivation
2019
An ESCRT-LEM protein surveillance system is poised to directly monitor the nuclear envelope and nuclear transport system
Thaller DJ, Allegretti M, Borah S, Ronchi P, Beck M, Lusk CP. An ESCRT-LEM protein surveillance system is poised to directly monitor the nuclear envelope and nuclear transport system. ELife 2019, 8: e45284. PMID: 30942170, PMCID: PMC6461442, DOI: 10.7554/elife.45284.Peer-Reviewed Original ResearchConceptsNuclear pore complexNPC assemblyNuclear membraneNuclear envelope barrierNuclear envelope herniationsNuclear envelope integrityNuclear transport systemXPO1/CRM1Membrane deliveryPore complexEnvelope integrityNuclear transportYeast modelNuclear poresChm7Nuclear envelopeFenestrated sheetHeh1Membrane disruptionMechanical membrane disruptionSelective barrierDisease mechanismsMembrane sealingTransport systemMembrane
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply