Structure/function relationships underlying regulation of FOXO transcription factors
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
18391969
DOI
10.1038/onc.2008.20
PII: onc200820
Knihovny.cz E-resources
- MeSH
- Acetylation MeSH
- Forkhead Transcription Factors chemistry physiology MeSH
- Phosphorylation MeSH
- Protein Conformation MeSH
- Humans MeSH
- Protein Processing, Post-Translational MeSH
- Ubiquitin metabolism MeSH
- Structure-Activity Relationship MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Forkhead Transcription Factors MeSH
- Ubiquitin MeSH
The FOXO subgroup of forkhead transcription factors plays a central role in cell-cycle control, differentiation, metabolism control, stress response and apoptosis. Therefore, the function of these important molecules is tightly controlled by a wide range of protein-protein interactions and posttranslational modifications including phosphorylation, acetylation and ubiquitination. The mechanisms by which these processes regulate FOXO activity are mostly elusive. This review focuses on recent advances in structural studies of forkhead transcription factors and the insights they provide into the mechanism of DNA recognition. On the basis of these data, we discuss structural aspects of protein-protein interactions and posttranslational modifications that target the forkhead domain and the nuclear localization signal of FOXO proteins.
References provided by Crossref.org
Structural plasticity of the FOXO-DBD:p53-TAD interaction
FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA
