Fol. Biol. 2024, 70, 152-165
Heat Shock Protein Network: the Mode of Action, the Role in Protein Folding and Human Pathologies
Protein folding is an extremely complicated process, which has been extensively tackled during the last decades. In vivo, a certain molecular machinery is responsible for assisting the correct folding of proteins and maintaining protein homeostasis: the members of this machinery are the heat shock proteins (HSPs), which belong among molecular chaperones. Mutations in HSPs are associated with several inherited diseases, and members of this group were also proved to be involved in neurodegenerative pathologies (e.g., Alzheimer and Parkinson diseases), cancer, viral infections, and antibiotic resistance of bacteria. Therefore, it is critical to understand the principles of HSP functioning and their exact role in human physiology and pathology. This review attempts to briefly describe the main chaperone families and the interplay between individual chaperones, as well as their general and specific functions in the context of cell physiology and human diseases.
Keywords
HSP, protein folding, chaperone, aggregation, neurodegenerative disease, cancer.
Funding
This study was supported by the Czech Science Foundation (22-27695S) and by the National Institute for Neurological Research (Programme EXCELES, ID Project No. LX22NPO5107) – Funded by the European Union – Next Generation EU. Additional institutional support from the Academy of Sciences of the Czech Republic (RVO: 61388971) is gratefully acknowledged.
References
Copyright
This is an open-access article distributed under the terms of the Creative Commons Attribution License.