SUMOylation, aging and autophagy in neurodegeneration

Neurotoxicology
Shamini Vijayakumaran, Dean L Pountney

Abstract

Protein homeostasis is essential for the wellbeing of several cellular systems. Post-translational modifications (PTM) coordinate various pathways in response to abnormal aggregation of proteins in neurodegenerative disease states. In the presence of accumulating misfolded proteins and toxic aggregates, the small ubiquitin-like modifier (SUMO) is associated with various substrates, including chaperones and other recruited factors, for refolding and for clearance via proteolytic systems, such as the ubiquitin-proteasome pathway (UPS), chaperone-mediated autophagy (CMA) and macroautophagy. However, these pathological aggregates are also known to inhibit both the UPS and CMA, further creating a toxic burden on cells. This review suggests that re-routing cytotoxic aggregates towards selective macroautophagy by modulating the SUMO pathway could provide new mechanisms towards neuroprotection.

Citations

Jan 12, 2019·Journal of Neuroscience Research·Silvia VanniGiuseppe Legname
Oct 18, 2019·Frontiers in Neuroscience·Dario ValdinocciDean L Pountney
Jan 31, 2019·Frontiers in Neuroscience·Cristine Alves da CostaFrédéric Checler
Jan 21, 2021·Proceedings of the National Academy of Sciences of the United States of America·Eva L MorozkoLeslie M Thompson
Mar 3, 2021·Cell Biochemistry and Function·Fathima Hajee BashaHemalatha Srinivasan
Mar 30, 2021·Ageing Research Reviews·Rohan GuptaPravir Kumar
Aug 7, 2021·Biomolecules·Iman F Fergani, Luciana R Frick

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