Researcher:
Elbeyli, Efe

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PhD Student

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Efe

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Elbeyli

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Elbeyli, Efe

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2018 - 201912020 - 20211

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Researcher Of Publications: search.filters.isAuthorOfPublication.49c81762-65e6-47be-8042-d5697f62f313

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    Anti-apoptotic bag-1S isoform is involved in endoplasmic reticulum associated degradation
    (Wiley, 2018) Can, Nisan Denizce; Akgun, Tugba Kizilboga; Dingiloglu, Baran; Doganay, Gizem Dinler; N/A; N/A; Department of Chemical and Biological Engineering; Muratçıoğlu, Serena; Elbeyli, Efe; Keskin, Özlem; PhD Student; PhD Student; Faculty Member; Department of Chemical and Biological Engineering; Graduate School of Sciences and Engineering; Graduate School of Sciences and Engineering; College of Engineering; N/A; N/A; 26605
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    PublicationOpen Access
    Interactome analysis of Bag-1 isoforms reveals novel interaction partners in endoplasmic reticulum-associated degradation
    (Public Library of Science, 2021) Can, Nisan Denizce; Baştürk, Ezgi; Kızılboğa, Tuğba; Akçay, İzzet Mehmet; Dingiloğlu, Baran; Tatlı, Özge; Acar, Sevilay; Kılbaş, Pelin Özfiliz; Jannuzzi, Ayşe Tarbin; Doğanay, Hamdi Levent; Yılmaz, Betül Karademir; Doğanay, Gizem Dinler; Department of Computer Engineering; Department of Chemical and Biological Engineering; Gürsoy, Attila; Keskin, Özlem; Elbeyli, Efe; Muratçıoğlu, Serena; Faculty Member; Department of Computer Engineering; Department of Chemical and Biological Engineering; College of Engineering; 8745; 26605; N/A; N/A
    Bag-1 is a multifunctional protein that regulates Hsp70 chaperone activity, apoptosis, and proliferation. The three major Bag-1 isoforms have different subcellular localizations and partly non-overlapping functions. To identify the detailed interaction network of each isoform, we utilized mass spectrometry-based proteomics and found that interactomes of Bag-1 isoforms contained many common proteins, with variations in their abundances. Bag-1 interactomes were enriched with proteins involved in protein processing and degradation pathways. Novel interaction partners included VCP/p97; a transitional ER ATPase, Rad23B; a shuttling factor for ubiquitinated proteins, proteasome components, and ER-resident proteins, suggesting a role for Bag-1 also in ER-associated protein degradation (ERAD). Bag-1 pull-down from cells and tissues from breast cancer patients validated these interactions and showed cancer-related prominence. Using in silico predictions we detected hotspot residues of Bag-1. Mutations of these residues caused loss of binding to protein quality control elements and impaired proteasomal activity in MCF-7 cells. Following CD147 glycosylation pattern, we showed that Bag-1 downregulated VCP/p97-dependent ERAD. Overall, our data extends the interaction map of Bag-1, and broadens its role in protein homeostasis. Targeting the interaction surfaces revealed in this study might be an effective strategy in the treatment of cancer.