Show simple item record

dc.contributor.authorSon, Sung Min
dc.contributor.authorPark, So Jung
dc.contributor.authorFernandez-Estevez, Marian
dc.contributor.authorRubinsztein, David C.
dc.date.accessioned2021-02-03T16:16:19Z
dc.date.available2021-02-03T16:16:19Z
dc.date.issued2021-01-22
dc.date.submitted2020-11-16
dc.identifier.issn1226-3613
dc.identifier.others12276-021-00556-4
dc.identifier.other556
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/317089
dc.descriptionFunder: 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.abstractAbstract: 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.languageen
dc.publisherNature Publishing Group UK
dc.rightsAttribution 4.0 International (CC BY 4.0)en
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subjectReview Article
dc.subject/631/80/458/1275
dc.subject/692/699/375/132/1283
dc.subjectreview-article
dc.titleAutophagy regulation by acetylation—implications for neurodegenerative diseases
dc.typeArticle
dc.date.updated2021-02-03T16:16:19Z
prism.endingPage41
prism.issueIdentifier1
prism.publicationNameExperimental & Molecular Medicine
prism.startingPage30
prism.volume53
dc.identifier.doi10.17863/CAM.64199
dcterms.dateAccepted2020-11-27
rioxxterms.versionofrecord10.1038/s12276-021-00556-4
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidRubinsztein, David C. [0000-0001-5002-5263]
dc.identifier.eissn2092-6413
pubs.funder-project-idAlzheimer’ Research UK (ARUK) (n/a)


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record

Attribution 4.0 International (CC BY 4.0)
Except where otherwise noted, this item's licence is described as Attribution 4.0 International (CC BY 4.0)