Autophagy regulation by acetylation—implications for neurodegenerative diseases
| dc.contributor.author | Son, Sung Min | |
| dc.contributor.author | Park, So Jung | |
| dc.contributor.author | Fernandez-Estevez, Marian | |
| dc.contributor.author | Rubinsztein, David C. | |
| dc.contributor.orcid | Rubinsztein, David C. [0000-0001-5002-5263] | |
| dc.date.accessioned | 2021-02-03T16:16:19Z | |
| dc.date.available | 2021-02-03T16:16:19Z | |
| dc.date.issued | 2021-01-22 | |
| dc.date.submitted | 2020-11-16 | |
| dc.date.updated | 2021-02-03T16:16:19Z | |
| dc.description | Funder: UK Dementia Research Institute (funded by the MRC, Alzheimer’s Research UK and the Alzheimer’s Society) Cambridge Centre for Parkinson-Plus National Institute for Health Research Cambridge Biomedical Research Centre | |
| dc.description.abstract | Abstract: Posttranslational modifications of proteins, such as acetylation, are essential for the regulation of diverse physiological processes, including metabolism, development and aging. Autophagy is an evolutionarily conserved catabolic process that involves the highly regulated sequestration of intracytoplasmic contents in double-membrane vesicles called autophagosomes, which are subsequently degraded after fusing with lysosomes. The roles and mechanisms of acetylation in autophagy control have emerged only in the last few years. In this review, we describe key molecular mechanisms by which previously identified acetyltransferases and deacetylases regulate autophagy. We highlight how p300 acetyltransferase controls mTORC1 activity to regulate autophagy under starvation and refeeding conditions in many cell types. Finally, we discuss how altered acetylation may impact various neurodegenerative diseases in which many of the causative proteins are autophagy substrates. These studies highlight some of the complexities that may need to be considered by anyone aiming to perturb acetylation under these conditions. | |
| dc.identifier.doi | 10.17863/CAM.64199 | |
| dc.identifier.eissn | 2092-6413 | |
| dc.identifier.issn | 1226-3613 | |
| dc.identifier.other | s12276-021-00556-4 | |
| dc.identifier.other | 556 | |
| dc.identifier.uri | https://www.repository.cam.ac.uk/handle/1810/317089 | |
| dc.language | en | |
| dc.publisher | Nature Publishing Group UK | |
| dc.rights | Attribution 4.0 International (CC BY 4.0) | en |
| dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | en |
| dc.subject | Review Article | |
| dc.subject | /631/80/458/1275 | |
| dc.subject | /692/699/375/132/1283 | |
| dc.subject | review-article | |
| dc.title | Autophagy regulation by acetylation—implications for neurodegenerative diseases | |
| dc.type | Article | |
| dcterms.dateAccepted | 2020-11-27 | |
| prism.endingPage | 41 | |
| prism.issueIdentifier | 1 | |
| prism.publicationName | Experimental & Molecular Medicine | |
| prism.startingPage | 30 | |
| prism.volume | 53 | |
| pubs.funder-project-id | Alzheimer’ Research UK (ARUK) (n/a) | |
| rioxxterms.licenseref.uri | http://creativecommons.org/licenses/by/4.0/ | |
| rioxxterms.version | VoR | |
| rioxxterms.versionofrecord | 10.1038/s12276-021-00556-4 |
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