pone.0256640.g003.tif (876.21 kB)
Bag-1 isoforms interact with protein quality control elements in breast cell lines and tissues.
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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 Doganaya. Immunoblotting assays for interaction partners of purified Bag-1S, M and L proteins extracted from MCF-7 and MCF-12A. Total, unbound, and Bag-1-bound protein extracts were blotted for BiP, PDIA3, Hsp70, Hsp90, VCP/p97, Rad23B, Calnexin and Calreticulin. b. Immunocytochemistry for assessment of Bag-1’s co-localization with interaction partners. MCF-7 cells transfected with Bag-1 isoforms were stained with Bag-1 antibody and VCP/p97. c. Co-immunoprecipitation assay in tissues from breast cancer patients. Interaction of Bag-1 with VCP/p97, Rad23B, and Hsp70 was increased in tumor tissues compared to normal. n = 4 for each molecular subtype of breast cancer. T: Tumor tissue, N: Neighboring normal tissue.
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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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