pone.0256640.g006.tif (163.89 kB)
Mutations on BAG and UbL domains affect proteasomal activity.
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posted on 2021-08-24, 17:29 authored by Nisan Denizce Can, Ezgi Basturk, Tugba Kizilboga, Izzet Mehmet Akcay, Baran Dingiloglu, Ozge Tatli, Sevilay Acar, Pelin Ozfiliz Kilbas, Efe Elbeyli, Serena Muratcioglu, Ayse Tarbin Jannuzzi, Attila Gursoy, Ozlem Keskin, Hamdi Levent Doganay, Betul Karademir Yilmaz, Gizem Dinler DoganayProteasome activity was measured by the fluorescence of released MCA in protein extracts from MCF-7 cells after transfection with a. Bag-1 isoforms and mock vector, and b. Bag-1S mutants and wild-type Bag-1S. Proteasome activity was measured under ATP-containing (grey) and ATP-depleted (orange) conditions. Significant differences were determined by t-test.
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ERADproteasome componentsER-associated protein degradationinteraction mapprotein homeostasisER ATPaseNovel interaction partnersmass spectrometry-based proteomicshotspot residuesMCF -7 cellsRad 23Bdegradation pathwaysprotein processingER-resident proteinssubcellular localizationsubiquitinated proteinssilico predictionsnovel interaction partnersisoformprotein quality control elementsmultifunctional proteininteraction networkproteasomal activityinteraction surfacesInteractome analysisBag -1. Mutationsbreast cancer patientsnon-overlapping functionsCD 147 glycosylation patternHsp 70 chaperone activityVCPendoplasmic reticulum-associated de...
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