Abstract
All heat shock protein (Hsp)70 molecular chaperones use the same fundamental biochemical mechanism of action, cycles of interaction with client proteins driven by adenosine triphosphate (ATP) binding and hydrolysis to maintain cellular proteostasis. However, they do not function alone; the action of co-chaperones is required. Together with Hsp70s, the J-proteins and nucleotide exchange factors (NEF) co-chaperones form Hsp70 networks. These networks are complex assembles with the number of components and their mutual interactions varying from species to species. Here, we consider Hsp70 networks functioning in a single cell eukaryote, baker’s yeast. By combining network theory perspective with available functional data and evolutionary analysis, we argue that it is possible to make sense of these complexities.
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Abbreviations
- ER:
-
Endoplasmic reticulum
- ERAD:
-
ER-associated degradation
- IMS:
-
Intermembrane space domain
- mtDNA:
-
Mitochondrial deoxyribonucleic acid (DNA)
- mtHsp70:
-
Mitochondrial heat shock protein (Hsp)70
- NBD:
-
Nucleotide-binding domain
- NEF:
-
Nucleotide exchange factor
- PDR:
-
Pleiotropic drug resistance
- RAC:
-
Ribosome-associated complex
- SBD:
-
Substrate-binding domain
- WGD:
-
Whole genome duplication
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Acknowledgments
Work in the laboratory of E.A. Craig was supported by the National Institutes of Health grants GM31107 and GM27870 (E.A.C.); work in the laboratory of J. Marszalek was supported by Foundation for Polish Science grant TEAM/2009−3/5 and Polish National Science Center grant Maestro DEC-2012/06/A/NZ1/000
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Craig, E., Marszalek, J. (2014). Yeast Hsp70 and J-protein Chaperones: Function and Interaction Network. In: Houry, W. (eds) The Molecular Chaperones Interaction Networks in Protein Folding and Degradation. Interactomics and Systems Biology, vol 1. Springer, New York, NY. https://doi.org/10.1007/978-1-4939-1130-1_3
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