FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00556576" target="_blank" >RIV/61388963:_____/22:00556576 - isvavai.cz</a>
Alternative codes found
RIV/67985823:_____/22:00556576 RIV/00216208:11310/22:10446733 RIV/00216224:14740/22:00128772
Result on the web
<a href="https://doi.org/10.1002/pro.4287" target="_blank" >https://doi.org/10.1002/pro.4287</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/pro.4287" target="_blank" >10.1002/pro.4287</a>
Alternative languages
Result language
angličtina
Original language name
FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA
Original language description
Transcription factor p53 protects cells against tumorigenesis when subjected to various cellular stresses. Under these conditions, p53 interacts with transcription factor Forkhead box O (FOXO) 4, thereby inducing cellular senescence by upregulating the transcription of senescence-associated protein p21. However, the structural details of this interaction remain unclear. Here, we characterize the interaction between p53 and FOXO4 by NMR, chemical cross-linking, and analytical ultracentrifugation. Our results reveal that the interaction between p53 TAD and the FOXO4 Forkhead domain is essential for the overall stability of the p53:FOXO4 complex. Furthermore, contacts involving the N-terminal segment of FOXO4, the C-terminal negative regulatory domain of p53 and the DNA-binding domains of both proteins stabilize the complex, whose formation blocks p53 binding to DNA but without affecting the DNA-binding properties of FOXO4. Therefore, our structural findings may help to understand the intertwined functions of p53 and FOXO4 in cellular homeostasis, longevity, and stress response.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GA21-02080S" target="_blank" >GA21-02080S: Molecular basis of interaction between FOXO Forkhead transcription factors and tumor suppressor p53</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein Science
ISSN
0961-8368
e-ISSN
1469-896X
Volume of the periodical
31
Issue of the periodical within the volume
5
Country of publishing house
US - UNITED STATES
Number of pages
13
Pages from-to
e4287
UT code for WoS article
000788245500005
EID of the result in the Scopus database
2-s2.0-85129098228