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Article

BAG3 Proteomic Signature under Proteostasis Stress

1
Institute of Pathobiochemistry, The Autophagy Lab, University Medical Center of the Johannes Gutenberg University, Duesbergweg 6, 55128 Mainz, Germany
2
Institute of Biochemistry II, Faculty of Medicine, Goethe University, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Current address: AbbVie Deutschland GmbH & Co. KG, Knollstraße 50, 67061 Ludwigshafen, Germany
§
Current address: Institute of Biochemistry, Medizinische Hochschule Brandenburg Theodor Fontane, Hochstrasse 29, 14770 Brandenburg/Havel, Germany
Current address: Munich Cluster for Systems Neurology (SyNergy), Medical Faculty, Ludwig-Maximilians-University München, Feodor-Lynen Strasse 17, 81377 Munich, Germany
Cells 2020, 9(11), 2416; https://doi.org/10.3390/cells9112416
Received: 13 October 2020 / Revised: 28 October 2020 / Accepted: 31 October 2020 / Published: 4 November 2020
The multifunctional HSP70 co-chaperone BAG3 (BCL-2-associated athanogene 3) represents a key player in the quality control of the cellular proteostasis network. In response to stress, BAG3 specifically targets aggregation-prone proteins to the perinuclear aggresome and promotes their degradation via BAG3-mediated selective macroautophagy. To adapt cellular homeostasis to stress, BAG3 modulates and functions in various cellular processes and signaling pathways. Noteworthy, dysfunction and deregulation of BAG3 and its pathway are pathophysiologically linked to myopathies, cancer, and neurodegenerative disorders. Here, we report a BAG3 proteomic signature under proteostasis stress. To elucidate the dynamic and multifunctional action of BAG3 in response to stress, we established BAG3 interactomes under basal and proteostasis stress conditions by employing affinity purification combined with quantitative mass spectrometry. In addition to the identification of novel potential BAG3 interactors, we defined proteins whose interaction with BAG3 was altered upon stress. By functional annotation and protein-protein interaction enrichment analysis of the identified potential BAG3 interactors, we confirmed the multifunctionality of BAG3 and highlighted its crucial role in diverse cellular signaling pathways and processes, ensuring cellular proteostasis and cell viability. These include protein folding and degradation, gene expression, cytoskeleton dynamics (including cell cycle and transport), as well as granulostasis, in particular. View Full-Text
Keywords: BAG3; proteostasis; protein quality control; stress response; autophagy; interactome BAG3; proteostasis; protein quality control; stress response; autophagy; interactome
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MDPI and ACS Style

Hiebel, C.; Stürner, E.; Hoffmeister, M.; Tascher, G.; Schwarz, M.; Nagel, H.; Behrends, C.; Münch, C.; Behl, C. BAG3 Proteomic Signature under Proteostasis Stress. Cells 2020, 9, 2416. https://doi.org/10.3390/cells9112416

AMA Style

Hiebel C, Stürner E, Hoffmeister M, Tascher G, Schwarz M, Nagel H, Behrends C, Münch C, Behl C. BAG3 Proteomic Signature under Proteostasis Stress. Cells. 2020; 9(11):2416. https://doi.org/10.3390/cells9112416

Chicago/Turabian Style

Hiebel, Christof, Elisabeth Stürner, Meike Hoffmeister, Georg Tascher, Mario Schwarz, Heike Nagel, Christian Behrends, Christian Münch, and Christian Behl. 2020. "BAG3 Proteomic Signature under Proteostasis Stress" Cells 9, no. 11: 2416. https://doi.org/10.3390/cells9112416

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