Abstract
Protein degradation is tightly regulated inside cells because of its utmost importance for protein homeostasis (proteostasis). The two major intracellular proteolytic pathways are the ubiquitin-proteasome and the autophagy-lysosome systems which ensure the fate of proteins when modified by various members of the ubiquitin family. These pathways are tightly interconnected by receptors and cofactors that recognize distinct chain architectures to connect with either the proteasome or autophagy under distinct physiologic and pathologic situations. The degradation of proteasome by autophagy, known as proteaphagy, plays an important role in this crosstalk since it favours the activity of autophagy in the absence of fully active proteasomes. Recently described in several biological models, proteaphagy appears to help the cell to survive when proteostasis is broken by the absence of nutrients or the excess of proteins accumulated under various stress conditions. Emerging evidence indicates that proteaphagy could be permanently activated in some types of cancer or when chemoresistance is observed in patients.
Highlights
In order to maintain cell viability, protein homeostasis needs to be tightly controlled.Proteostasis is regulated by many mechanisms, including various post-translational modifications (PTM)
30 autophagy receptors known so far in mammalians, functional domains are observed such as the presence of ubiquitin binding domains (UBDs), ATG8sdomains (UBDs), ATG8s binding domains like LC3 structural similarities and preserved functional domains are observed such as theAggrephagy presence of; ubiquitin binding
Maintaining the cellular proteostasis is of the upmost importance for cells health
Summary
In order to maintain cell viability, protein homeostasis (proteostasis) needs to be tightly controlled. The ubiquitin proteasome system (UPS) is one of the main mechanisms for intracellular protein controlled, to ensure the correct turnover of substrates involved in a wide variety of cellular degradation and is essential to maintain protein homeostasis. Protein ubiquitylation and degradation is tightly the modification/de-modification of substrates, chaperones and permanent or transient components regulated by a large number of cellular factors including Ub and UbL, enzymes involved in the of the proteasome [11,12]. Modification/de-modification of substrates, chaperones and permanent or transient components of the proteasome [11,12]
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