Deciphering the acetylation code of p53 in transcription regulation and tumor suppression.
Journal
Oncogene
ISSN: 1476-5594
Titre abrégé: Oncogene
Pays: England
ID NLM: 8711562
Informations de publication
Date de publication:
05 2022
05 2022
Historique:
received:
03
03
2022
accepted:
20
04
2022
revised:
14
04
2022
pubmed:
30
4
2022
medline:
31
5
2022
entrez:
29
4
2022
Statut:
ppublish
Résumé
Although it is well-established that p53-mediated tumor suppression mainly acts through its ability in transcriptional regulation, the molecular mechanisms of this regulation are not completely understood. Among a number of regulatory modes, acetylation of p53 attracts great interests. p53 was one of the first non-histone proteins found to be functionally regulated by acetylation and deacetylation, and subsequent work has established that reversible acetylation is a general mechanism for regulation of non-histone proteins. Unlike other types of posttranslational modifications occurred during stress responses, the role of p53 acetylation has been recently validated in vivo by using the knock-in mice with both acetylation-defective and acetylation-mimicking p53 mutants. Here, we review the role of acetylation in p53-mediated activities, with a focus on which specific acetylation sites are critical for p53-dependent transcription regulation during tumor suppression and how acetylation of p53 recruits specific "readers" to execute its promoter-specific regulation of different targets. We also discuss the role of p53 acetylation in differentially regulating its classic activities in cell cycle arrest, senescence and apoptosis as well as newly identified unconventional functions such as cell metabolism and ferroptosis.
Identifiants
pubmed: 35487975
doi: 10.1038/s41388-022-02331-9
pii: 10.1038/s41388-022-02331-9
pmc: PMC9149126
mid: NIHMS1800386
doi:
Substances chimiques
Trp53 protein, mouse
0
Tumor Suppressor Protein p53
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
3039-3050Subventions
Organisme : NCI NIH HHS
ID : R01 CA254970
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA258390
Pays : United States
Organisme : NCI NIH HHS
ID : R35 CA253059
Pays : United States
Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer Nature Limited.
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