Commentary 10.1172/JCI95839

BAG3 plays a central role in proteostasis in the heart

Wataru Mizushima and Junichi Sadoshima

Department of Cell Biology and Molecular Medicine, Cardiovascular Research Institute, Rutgers New Jersey Medical School, Newark, New Jersey, USA.

Address correspondence to: Junichi Sadoshima, Rutgers New Jersey Medical School, Department of Cell Biology and Molecular Medicine, 185 South Orange Ave, MSB G-609, Newark, New Jersey 07103, USA. Phone: 973.972.8920; Email: sadoshju@njms.rutgers.edu.

Find articles by Mizushima, W. in: JCI | PubMed | Google Scholar

Department of Cell Biology and Molecular Medicine, Cardiovascular Research Institute, Rutgers New Jersey Medical School, Newark, New Jersey, USA.

Address correspondence to: Junichi Sadoshima, Rutgers New Jersey Medical School, Department of Cell Biology and Molecular Medicine, 185 South Orange Ave, MSB G-609, Newark, New Jersey 07103, USA. Phone: 973.972.8920; Email: sadoshju@njms.rutgers.edu.

Find articles by Sadoshima, J. in: JCI | PubMed | Google Scholar

First published July 24, 2017 - More info

Published in Volume 127, Issue 8 (August 1, 2017)
J Clin Invest. 2017;127(8):2900–2903. doi:10.1172/JCI95839.
Copyright © 2017, American Society for Clinical Investigation

First published July 24, 2017

See the related article at Loss-of-function mutations in co-chaperone BAG3 destabilize small HSPs and cause cardiomyopathy.

Proteinopathies are characterized by the accumulation of misfolded proteins, which ultimately interfere with normal cell function. While neurological diseases, such as Huntington disease and Alzheimer disease, are well-characterized proteinopathies, cardiac diseases have recently been associated with alterations in proteostasis. In this issue of the JCI, Fang and colleagues demonstrate that mice with cardiac-specific deficiency of the co-chaperone protein BCL2-associated athanogene 3 (BAG3) develop dilated cardiomyopathy that is associated with a destabilization of small HSPs as the result of a disrupted interaction between BAG3 and HSP70. Together, the results of this study suggest that strategies to upregulate BAG3 during cardiac dysfunction may be beneficial.

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