BAG2 structure, function and involvement in disease

Cell Mol Biol Lett. 2016 Sep 20:21:18. doi: 10.1186/s11658-016-0020-2. eCollection 2016.

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.

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

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Molecular Chaperones / metabolism*
  • Molecular Chaperones / physiology
  • Neoplasms / metabolism
  • Neoplasms / pathology
  • Neurodegenerative Diseases / metabolism
  • Neurodegenerative Diseases / pathology
  • Protein Conformation

Substances

  • BAG2 protein, human
  • Molecular Chaperones