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

Grégoire Quinet (1, 2) , Maria Gonzalez-Santamarta (1, 2) , Clara Louche (1, 2) , Manuel S Rodriguez (1, 2)

1 ITAV - Institut des Technologies Avancées en sciences du Vivant
2 IPBS - Institut de pharmacologie et de biologie structurale

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.

Mots clés: Ubiquitin proteasome system; Autophagy; Ubiquitin-like; Proteaphagy; Pathology; Ubiquitin proteasome system

Domaines: Biochimie, Biologie Moléculaire

Grégoire Quinet, Maria Gonzalez-Santamarta, Clara Louche, Manuel S Rodriguez. Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy. Molecules, 2020, 25 (10), pp.2352. ⟨10.3390/molecules25102352⟩. ⟨hal-03006987⟩