Fam83F induces p53 stabilisation and promotes its activity
File(s)
Author(s)
Type
Journal Article
Abstract
p53 is one of the most important tumour suppressor proteins currently known. It is activated in response to DNA damage and this activation leads to proliferation arrest and cell death. The abundance and activity of p53 are tightly controlled and reductions in p53's activity can contribute to the development of cancer. Here, we show that Fam83F increases p53 protein levels by protein stabilisation. Fam83F interacts with p53 and decreases its ubiquitination and degradation. Fam83F is induced in response to DNA damage and its overexpression also increases p53 activity in cell culture experiments and in zebrafish embryos. Downregulation of Fam83F decreases transcription of p53 target genes in response to DNA damage and increases cell proliferation, identifying Fam83F as an important regulator of the DNA damage response. Overexpression of Fam83F also enhances migration of cells harbouring mutant p53 demonstrating that it can also activate mutant forms of p53.
Date Issued
2019-01-28
Date Acceptance
2019-01-09
Citation
Cell Death and Differentiation, 2019, 26, pp.2125-2138
ISSN
1350-9047
Publisher
Springer Nature [academic journals on nature.com]
Start Page
2125
End Page
2138
Journal / Book Title
Cell Death and Differentiation
Volume
26
Copyright Statement
© 2019 ADMC Associazione Differenziamento e Morte Cellulare. The final publication is available at Springer Nature via https://dx.doi.org/10.1038/s41418-019-0281-1
Identifier
https://www.ncbi.nlm.nih.gov/pubmed/30692643
PII: 10.1038/s41418-019-0281-1
Subjects
Science & Technology
Life Sciences & Biomedicine
Biochemistry & Molecular Biology
Cell Biology
MDM2
UBIQUITINATION
DEGRADATION
LIGASE
GROWTH
Biochemistry & Molecular Biology
06 Biological Sciences
11 Medical and Health Sciences
Publication Status
Published
Coverage Spatial
England
Date Publish Online
2019-01-28