0000000000745069

AUTHOR

Karin Awe

showing 2 related works from this author

Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.

2008

AbstractThe hepatitis B virus L protein forms a dual topology in the endoplasmic reticulum (ER) via a process involving cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain. Here, we show that preS posttranslocation depends on the action of the ER chaperone BiP. To modulate the in vivo BiP activity, we designed an approach based on overexpressing its positive and negative regulators, ER-localized DnaJ-domain containing protein 4 (ERdj4) and BiP-associated protein (BAP), respectively. The feasibility of this approach was confirmed by demonstrating that BAP, but not ERdj4, destabilizes the L/BiP complex. Overexpressing BAP or ERdj4 inhibits…

Hepatitis B virusgenetic structuresBiPBiophysicsHemagglutinin (influenza)Chromosomal translocationmacromolecular substancesmedicine.disease_causeEndoplasmic ReticulumBiochemistryCell LineAdenosine TriphosphateViral Envelope ProteinsStructural BiologyIn vivoCalnexinHBVGeneticsmedicineHumansMolecular BiologyEndoplasmic Reticulum Chaperone BiPTranslocational regulationHeat-Shock ProteinsHepatitis B virusbiologyEndoplasmic reticulumMembrane ProteinsCell BiologyHSP40 Heat-Shock ProteinsMolecular biologyProtein Structure TertiaryProtein TransportDual topologyMembrane topologyProtein BiosynthesisMembrane topologybiology.proteinPosttranslational translocationMolecular ChaperonesFEBS letters
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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
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