0000000000793950

AUTHOR

Katherina Gotthardt

showing 2 related works from this author

γ2-Adaptin is functioning in the late endosomal sorting pathway and interacts with ESCRT-I and -III subunits.

2010

Abstractγ2-Adaptin is a clathrin adaptor-related protein with unclear physiological function. Previous studies indicated that γ2-adaptin might act within the multivesicular body (MVB) protein-sorting pathway that is central to receptor down-regulation, lysosome biogenesis, and budding of enveloped viruses. Here, we have analyzed the effects of excess and deficit γ2-adaptin on exogenous and endogenous MVB cargoes and on the MVB machinery itself. Foreign cargoes, like retroviral Gags, are entrapped by overexpressed γ2-adaptin in detergent-insoluble polymers and blocked in budding. When viral budding involves MVB/endosomal structures, excess γ2-adaptin acts by accelerating lysosomal Gag destru…

EndosomeViral buddingImmunoblottingGene Products gagmacromolecular substancesEndosomesTransfectionClathrinESCRTLysosomeCell Line TumormedicineBiomarkers TumorHumansMultivesicular bodyMultivesicular BodyMolecular BiologyAdaptor Protein Complex gamma SubunitsBuddingbiologyEndosomal Sorting Complexes Required for TransportCHMP2AVirus buddingMultivesicular BodiesVps28Cell BiologyLysosomeCell biologyLuminescent ProteinsProtein Transportmedicine.anatomical_structureRetroviridaeMicroscopy Fluorescencebiology.proteinRNA InterferenceLysosomesBiogenesisProtein BindingSignal TransductionBiochimica et biophysica acta
researchProduct

Role of Human Sec63 in Modulating the Steady-State Levels of Multi-Spanning Membrane Proteins

2012

The Sec61 translocon of the endoplasmic reticulum (ER) membrane forms an aqueous pore, allowing polypeptides to be transferred across or integrated into membranes. Protein translocation into the ER can occur co- and posttranslationally. In yeast, posttranslational translocation involves the heptameric translocase complex including its Sec62p and Sec63p subunits. The mammalian ER membrane contains orthologs of yeast Sec62p and Sec63p, but their function is poorly understood. Here, we analyzed the effects of excess and deficit Sec63 on various ER cargoes using human cell culture systems. The overexpression of Sec63 reduces the steady-state levels of viral and cellular multi-spanning membrane …

Gastroenterology and hepatologylcsh:MedicineProtein SynthesisEndoplasmic ReticulumBiochemistryHepatitisViral Envelope ProteinsMolecular Cell BiologyTranslocaseRNA Small Interferinglcsh:ScienceIntegral membrane proteinEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyMembrane transport proteinReverse Transcriptase Polymerase Chain ReactionRNA-Binding ProteinsHepatitis BCellular StructuresCell biologyInfectious hepatitisCytochemistryMedicineInfectious diseasesResearch ArticleBlotting WesternViral diseasesReal-Time Polymerase Chain ReactionTransfectionCell LineSEC63Bacterial ProteinsHumansBiologyLiver diseasesDNA PrimersEndoplasmic reticulumlcsh:RCell MembraneMembrane ProteinsMembrane Transport ProteinsProteinsSEC61 TransloconChaperone ProteinsTransmembrane ProteinsLuminescent ProteinsMembrane proteinGene Expression RegulationMicroscopy FluorescenceSubcellular OrganellesChaperone (protein)Mutationbiology.proteinlcsh:QMolecular ChaperonesPLoS ONE
researchProduct