Search results for "JUNQ and IPOD"

showing 3 items of 3 documents

BAG3 and friends: co-chaperones in selective autophagy during aging and disease.

2011

There is a reciprocal change in the expression of two members of the BAG (Bcl-2-associated athanogen) family, BAG1 and BAG3, during cellular aging and under acute stress ("BAG1-BAG3-switch"). BAG3 was recently described as a mediator of a novel macroautophagy pathway that uses the specificity of heat shock protein 70 (HSP70) to misfolded proteins and also involves other protein partners, such as HSPB8. Also crucial for induction and execution of autophagy are sequestosome-1/p62 (SQSTM1/p62) and LC3, an autophagosome-associated protein. In this novel pathway, BAG3 mediates the targeting and transport of degradation-prone substrates into aggresomes via the microtubule-motor dynein. Interestin…

AgingProteasome Endopeptidase ComplexDyneinBAG3Models BiologicalJUNQ and IPODUbiquitinAutophagyAnimalsDiseaseMolecular BiologyAdaptor Proteins Signal TransducingbiologyAutophagyUbiquitinationSignal transducing adaptor proteinDyneinsCell BiologyAdaptation PhysiologicalCell biologyHsp70DNA-Binding ProteinsAggresomeBiochemistrybiology.proteinMolecular ChaperonesTranscription FactorsAutophagy
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BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins.

2010

Increasing evidence indicates the existence of selective autophagy pathways, but the manner in which substrates are recognized and targeted to the autophagy system is poorly understood. One strategy is transport of a particular substrate to the aggresome, a perinuclear compartment with high autophagic activity. In this paper, we identify a new cellular pathway that uses the specificity of heat-shock protein 70 (Hsp70) to misfolded proteins as the basis for aggresome-targeting and autophagic degradation. This pathway is regulated by the stress-induced co-chaperone Bcl-2-associated athanogene 3 (BAG3), which interacts with the microtubule-motor dynein and selectively directs Hsp70 substrates …

Protein FoldingRecombinant Fusion ProteinsDyneinGreen Fluorescent ProteinsAggrephagyMice TransgenicBAG3BiochemistryMiceJUNQ and IPODChlorocebus aethiopsGeneticsAutophagyAnimalsHumansPoint MutationHSP70 Heat-Shock ProteinsMolecular BiologyAdaptor Proteins Signal TransducingSequence DeletionInclusion BodiesMotor NeuronsbiologySuperoxide DismutaseAutophagyScientific ReportsDyneinsTransport proteinCell biologyProtein TransportAggresomeHEK293 CellsSpinal CordChaperone (protein)COS Cellsbiology.proteinApoptosis Regulatory ProteinsProteasome InhibitorsEMBO reports
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2017

Human neurodegenerative diseases are accompanied by accumulation of heavily oxidized and aggregated proteins. However, the exact molecular reason is not fully elucidated yet. Insufficient cellular protein quality control is thought to play an important role in accumulating covalently oxidized misfolded proteins. Pharmacologically active polyphenols and their derivatives exhibit potential for preventive and therapeutic purposes against protein aggregation during neurodegeneration. Although these compounds act on various biochemical pathways, their role in stabilizing the protein degradation machinery at different stages may be an attractive therapeutical strategy to halt the accumulation of …

0301 basic medicineOrganic ChemistryNeurodegenerationPharmaceutical ScienceProtein aggregationProtein degradationBiologymedicine.diseaseProtein oxidationAnalytical ChemistryCell biology03 medical and health sciences030104 developmental biologyChaperone-mediated autophagyProteostasisJUNQ and IPODBiochemistryProteasomeChemistry (miscellaneous)Drug DiscoverymedicineMolecular MedicinePhysical and Theoretical ChemistryMolecules
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