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Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy

ITAV-CNRS USR 3505 IPBS-UPS, 1 place Pierre Potier, 31106 Toulouse, France
Author to whom correspondence should be addressed.
Molecules 2020, 25(10), 2352;
Received: 26 April 2020 / Revised: 14 May 2020 / Accepted: 16 May 2020 / Published: 18 May 2020
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.
Keywords: ubiquitin proteasome system; autophagy; ubiquitin-like; proteaphagy; pathology ubiquitin proteasome system; autophagy; ubiquitin-like; proteaphagy; pathology
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MDPI and ACS Style

Quinet, G.; Gonzalez-Santamarta, M.; Louche, C.; Rodriguez, M.S. Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy. Molecules 2020, 25, 2352.

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