BAG2 structure, function and involvement in disease

Cellular & Molecular Biology Letters

Jifeng Guo²  Lixia Qin³  Hainan Zhang¹  Qian Zheng¹ 

[1] Department of Neurology, The Second Xiangya Hospital, Central South University, Changsha, China$$;Department of Neurology, Xiangya Hospital, Central South University, Changsha, China$$;Department of Neurology, The Second Xiangya Hospital, Central South University, Changsha, China$$Department of Neurology, Xiangya Hospital, Central South University, Changsha, China$$

关键词: BAG2;    Molecular chaperones;    Carcinoma;    Alzheimer’s disease;    Parkinson’s disease;    Spinocerebellar ataxia type-3;   

DOI  :  10.1186/s11658-016-0020-2

学科分类：分子生物学，细胞生物学和基因

来源: Uniwersytet Wroclawski * Wydzial Biotechnologii / University of Wroclaw, Faculty of Biotechnology

【 摘 要 】

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.

【 授权许可】

Unknown