Elucidation of Site-Specific Ubiquitination on Chaperones in Response to Mutant Huntingtin
Author:
Funder
Indian Council of Medical Research
Science and Engineering Research Board
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Cellular and Molecular Neuroscience,General Medicine
Link
https://link.springer.com/content/pdf/10.1007/s10571-023-01446-1.pdf
Reference65 articles.
1. Aktar F, Burudpakdee C, Polanco M, Pei S, Swayne TC, Lipke PN, Emtage L (2019) The huntingtin inclusion is a dynamic phase-separated compartment. Life Sci Alliance 2(5):e201900489. https://doi.org/10.26508/lsa201900489
2. Alberti S, Hyman AA (2021) Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing. Nat Rev Mol Cell Biol 22(3):196–213. https://doi.org/10.1038/s41580-020-00326-6
3. Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431(7010):805–810. https://doi.org/10.1038/nature02998
4. Backe SJ, Sager RA, Woodford MR, Makedon AM, Mollapour M (2020) Post-translational modifications of Hsp90 and translating the chaperone code. J Biol Chem 295(32):11099–11117. https://doi.org/10.1074/jbc.REV120.011833
5. Baker HA, Bernardini JP (2021) It’s not just a phase; ubiquitination in cytosolic protein quality control. Biochem Soc Trans 49(1):365–377. https://doi.org/10.1042/BST20200694
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