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RESEARCH PRODUCT
Breaking BAG: The Co-Chaperone BAG3 in Health and Disease.
Christian Behlsubject
0301 basic medicineProtein domainCellular homeostasisBiologyToxicologyBAG303 medical and health sciencesMuscular DiseasesNeoplasmsmedicineAutophagyAnimalsHumansHSP70 Heat-Shock ProteinsAdaptor Proteins Signal TransducingPharmacologyAutophagyNeurodegenerationNeurodegenerative Diseasesmedicine.diseaseCell biologyHsp70Co-chaperone030104 developmental biologyProteasomeApoptosis Regulatory Proteinsdescription
Human BAG ( B cl-2-associated a thano g ene) proteins form a family of antiapoptotic proteins that currently consists of six members (BAG1–6) all sharing the BAG protein domain from which the name arises. Via this domain, BAG proteins bind to the heat shock protein 70 (Hsp70), thereby acting as a co-chaperone regulating the activity of Hsp70. In addition to their antiapoptotic activity, all human BAG proteins have distinct functions in health and disease, and BAG3 in particular is the focus of many investigations. BAG3 has a modular protein domain composition offering the possibility for manifold interactions with other proteins. Various BAG3 functions are implicated in disorders including cancer, myopathies, and neurodegeneration. The discovery of its role in selective autophagy and the description of BAG3-mediated selective macroautophagy as an adaptive mechanism to maintain cellular homeostasis, under stress as well as during aging, make BAG3 a highly interesting target for future pharmacological interventions.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2016-08-01 | Trends in pharmacological sciences |