Abstract
Cellular protein homeostasis (proteostasis) is maintained by a broad network of proteins involved in synthesis, folding, triage, repair and degradation. Chief among these are molecular chaperones and their cofactors that act as powerful protein remodelers. The growing realization that many human pathologies are fundamentally diseases of protein misfolding (proteopathies) has generated interest in understanding how the proteostasis network impacts onset and progression of these diseases. In this minireview, we highlight recent progress in understanding the enigmatic Hsp110 class of heat shock protein that acts as both a potent nucleotide exchange factor to regulate activity of the foldase Hsp70, and as a passive chaperone capable of recognizing and binding cellular substrates on its own, and its integration into the proteostasis network.
Acknowledgments
We apologize to the many investigators whose contributions we were unable to cite due to the brevity of this minireview. Work in the authors’ laboratory was supported by NIH grants GM074696 (Funder Id: 10.13039/100000057), GM127287 and AG051046 (Funder Id: 10.13039/100000049).
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©2018 Walter de Gruyter GmbH, Berlin/Boston
Articles in the same Issue
- Frontmatter
- Highlight: sphingolipids in infectious biology and immunology
- Sphingolipids in early viral replication and innate immune activation
- The function of sphingomyelinases in mycobacterial infections
- The role of acid sphingomyelinase and modulation of sphingolipid metabolism in bacterial infection
- The neutral sphingomyelinase 2 in T cell receptor signaling and polarity
- Click reactions with functional sphingolipids
- Sphingolipids in inflammatory hypoxia
- CD4+ Foxp3+ regulatory T cell-mediated immunomodulation by anti-depressants inhibiting acid sphingomyelinase
- Pathological manifestations of Farber disease in a new mouse model
- Pulmonary infection of cystic fibrosis mice with Staphylococcus aureus requires expression of α-toxin
- Minireview
- Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding
- Research Articles/Short Communications
- Proteolysis
- The two cathepsin B-like proteases of Arabidopsis thaliana are closely related enzymes with discrete endopeptidase and carboxydipeptidase activities
Articles in the same Issue
- Frontmatter
- Highlight: sphingolipids in infectious biology and immunology
- Sphingolipids in early viral replication and innate immune activation
- The function of sphingomyelinases in mycobacterial infections
- The role of acid sphingomyelinase and modulation of sphingolipid metabolism in bacterial infection
- The neutral sphingomyelinase 2 in T cell receptor signaling and polarity
- Click reactions with functional sphingolipids
- Sphingolipids in inflammatory hypoxia
- CD4+ Foxp3+ regulatory T cell-mediated immunomodulation by anti-depressants inhibiting acid sphingomyelinase
- Pathological manifestations of Farber disease in a new mouse model
- Pulmonary infection of cystic fibrosis mice with Staphylococcus aureus requires expression of α-toxin
- Minireview
- Roles of the nucleotide exchange factor and chaperone Hsp110 in cellular proteostasis and diseases of protein misfolding
- Research Articles/Short Communications
- Proteolysis
- The two cathepsin B-like proteases of Arabidopsis thaliana are closely related enzymes with discrete endopeptidase and carboxydipeptidase activities