Abstract
Bcl2-associated athanogene 2 (BAG2) shares a similar molecular structure and function with other BAG family members. Functioning as a co-chaperone, it interacts with the ATPase domain of the heat shock protein 70 (dHsp70) through its BAG domain. It also interacts with many other molecules and regulates various cellular functions. An increasing number of studies have indicated that BAG2 is involved in the pathogenesis of various diseases, including cancers and neurodegenerative diseases. This paper is a comprehensive review of the structure, functions, and protein interactions of BAG2. We also discuss its roles in diseases, including cancer, Alzheimer’s disease, Parkinson’s disease and spinocerebellar ataxia type-3. Further research on BAG2 could lead to an understanding of the pathogenesis of these disorders or even to novel therapeutic approaches.
Highlights
The Bcl2-associated athanogene (BAG) (Bcl-2-associated athanogene) family was first identified as a group of proteins that prevent cell death through their interaction with Bcl-2 [1, 2]
Bcl2-associated athanogene 2 (BAG2) is an inhibitor of the Hsp70-binding E3 ubiquitin ligase Carboxyl-terminus of Hsp70-interacting protein (CHIP) [19]
Carrettiero et al found that cellular levels of BAG2 are directly under the physiological control of miR-128a [40, 41]. These findings suggest that downregulation of BAG2 by miR-128a leads to shunting of tau degradation toward the less efficient ubiquitin-dependent pathway, and the resulting decreased strength of BAG2-mediated tau degradation pathways [42] could confer risk for neurodegeneration [37]
Summary
The BAG (Bcl-2-associated athanogene) family was first identified as a group of proteins that prevent cell death through their interaction with Bcl-2 [1, 2]. It directly interacts through the BAG domain with the ATPase domain of Hsp70/Hsc70 molecular chaperones [3, 4]. BAG proteins can bind to various transcription factors and regulate a range of processes, including cell apoptosis, tumor growth, neuronal differentiation and the stress response [6, 7]. In a study that used a yeast two-hybrid approach, BAG2 was found to be an Hsp70/Hsc70 molecular chaperone-interacting protein [5].
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