Indispensable Role of Protein Turnover in Autophagy, Apoptosis and Ubiquitination Pathways
Heat-shock proteins (HSPs) have been engaged in versatile functions including chaperone activity, protein folding, apoptosis, autophagy and Ubiquitination. The cell safeguarded by a robust protein quality control mechanism which maintains protein homeosta
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, Eman A. M. Abd El Khalik
,
Abstract Introduction Heat-shock proteins (HSPs) have been engaged in versatile functions including chaperone activity, protein folding, apoptosis, autophagy and Ubiquitination. The cell safeguarded by a robust protein quality control mechanism which maintains protein homeostasis, also aka as proteostasis. Recent studies have described HSPs facilitate the folding process of newly synthesized peptides and the re-folding and recruitment process of functionalized proteins that are damaged under cellular stress, but they also participate with the degradation pathway of misfolded proteins to cope the demand of the cell. Additionally, whether a protein will be subjected to the folding or degradation process is determined by the protein quality control mechanism, which considered as a network of HSPs and degradation systems. The turnover of proteins is a representation of the balance between protein synthesis and degradation and is a vital mechanism for preserving the cellular protein pool. Protein folding, refolding of misfolded proteins or the degradation of misfolded and damaged proteins are part of protein quality control. In this chapter, we will be describing the prominent role of HSPs in protein turnover regulation; the effects of HSPs on protein degradation, apoptosis, autophagy, and the proteasome.
Afnan H. El-Gowily and Mohammed A. Abosheasha contributed equally to this study. M. A. Abosheasha (*) Cellular Genetics Laboratory, Graduate School of Science, Tokyo Metropolitan University, Tokyo, Japan e-mail: [email protected]; [email protected] E. A. M. Abd El Khalik Biochemistry Division, Chemistry Department, Faculty of science, Tanta University, Tanta, Egypt A. H. El-Gowily (*) Biochemistry Division, Chemistry Department, Faculty of science, Tanta University, Tanta, Egypt Organ and Cell physiology, Juntendo University, Tokyo, Japan e-mail: [email protected]; [email protected] © Springer Nature Switzerland AG 2020 A. A. A. Asea, P. Kaur (eds.), Heat Shock Proteins, https://doi.org/10.1007/7515_2020_31
M. A. Abosheasha et al.
Methods The authors conducted a narrative review of most relevant papers. Results Several studies also demonstrated the role of HSPs in protein turnover. As a while, there are various factors that control the correction of protein folding and degradation; the most important one is the heat shock protein family. Heat shock proteins (HSPs) are a molecular chaperone-type, which can avoid unwanted protein interactions and induce the proper folding. On the other hand, these proteins play essential roles in the pathways of protein degradation, the ubiquitin-proteasome system, apoptosis and autophagy. Conclusions Regarding to the different roles of HSPs and signaling pathways in biology and medicine, we described how these systems interact to maintain proteostasis; as well as the role of the protein quality control system, which offers a novel perspective on promising therapeutic strategies based on the differential role
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