Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy
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 m...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-05-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/25/10/2352 |
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| author | Grégoire Quinet Maria Gonzalez-Santamarta Clara Louche Manuel S. Rodriguez |
| author_facet | Grégoire Quinet Maria Gonzalez-Santamarta Clara Louche Manuel S. Rodriguez |
| author_sort | Grégoire Quinet |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T19:45:39Z |
| format | Article |
| id | doaj.art-55b2972f11164e33ae0d8b04acdc0381 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T19:45:39Z |
| publishDate | 2020-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-55b2972f11164e33ae0d8b04acdc03812023-11-20T00:50:40ZengMDPI AGMolecules1420-30492020-05-012510235210.3390/molecules25102352Mechanisms Regulating the UPS-ALS Crosstalk: The Role of ProteaphagyGrégoire Quinet0Maria Gonzalez-Santamarta1Clara Louche2Manuel S. Rodriguez3ITAV-CNRS USR 3505 IPBS-UPS, 1 Place Pierre Potier, 31106 Toulouse, FranceITAV-CNRS USR 3505 IPBS-UPS, 1 Place Pierre Potier, 31106 Toulouse, FranceITAV-CNRS USR 3505 IPBS-UPS, 1 Place Pierre Potier, 31106 Toulouse, FranceITAV-CNRS USR 3505 IPBS-UPS, 1 Place Pierre Potier, 31106 Toulouse, FranceProtein 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.https://www.mdpi.com/1420-3049/25/10/2352ubiquitin proteasome systemautophagyubiquitin-likeproteaphagypathology |
| spellingShingle | Grégoire Quinet Maria Gonzalez-Santamarta Clara Louche Manuel S. Rodriguez Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy Molecules ubiquitin proteasome system autophagy ubiquitin-like proteaphagy pathology |
| title | Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy |
| title_full | Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy |
| title_fullStr | Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy |
| title_full_unstemmed | Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy |
| title_short | Mechanisms Regulating the UPS-ALS Crosstalk: The Role of Proteaphagy |
| title_sort | mechanisms regulating the ups als crosstalk the role of proteaphagy |
| topic | ubiquitin proteasome system autophagy ubiquitin-like proteaphagy pathology |
| url | https://www.mdpi.com/1420-3049/25/10/2352 |
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