Version 1
: Received: 17 April 2024 / Approved: 17 April 2024 / Online: 17 April 2024 (14:47:03 CEST)
How to cite:
Będzińska, A.; Łasut-Szyszka, B.; Krześniak, M.; Gdowicz-Kłosok, A.; Rusin, M. Puzzling Regulation of Interferon Signaling System by p53 Tumor Suppressor Protein. Preprints2024, 2024041169. https://doi.org/10.20944/preprints202404.1169.v1
Będzińska, A.; Łasut-Szyszka, B.; Krześniak, M.; Gdowicz-Kłosok, A.; Rusin, M. Puzzling Regulation of Interferon Signaling System by p53 Tumor Suppressor Protein. Preprints 2024, 2024041169. https://doi.org/10.20944/preprints202404.1169.v1
Będzińska, A.; Łasut-Szyszka, B.; Krześniak, M.; Gdowicz-Kłosok, A.; Rusin, M. Puzzling Regulation of Interferon Signaling System by p53 Tumor Suppressor Protein. Preprints2024, 2024041169. https://doi.org/10.20944/preprints202404.1169.v1
APA Style
Będzińska, A., Łasut-Szyszka, B., Krześniak, M., Gdowicz-Kłosok, A., & Rusin, M. (2024). Puzzling Regulation of Interferon Signaling System by p53 Tumor Suppressor Protein. Preprints. https://doi.org/10.20944/preprints202404.1169.v1
Chicago/Turabian Style
Będzińska, A., Agnieszka Gdowicz-Kłosok and Marek Rusin. 2024 "Puzzling Regulation of Interferon Signaling System by p53 Tumor Suppressor Protein" Preprints. https://doi.org/10.20944/preprints202404.1169.v1
Abstract
The p53 tumor suppressor protein shows antiviral activity. The replication of viruses is also antagonized by interferons (IFNs) – cytokines, which control immunity genes by the STAT transcription factors. The best studied interferons belong to type I (e.g. IFNα) and type II (IFNγ) groups. IFNα and IFNγ both induce activating phosphorylation of STAT1 on Tyr701. Previously, we noticed that p53 activates SOCS1, which is a negative regulator of STAT1 phosphorylation. Thus, we hypothesized that p53 by activating SOCS1 expression reduces phosphorylation of STAT1 and attenuates activation of genes stimulated either by IFNα or IFNγ. To test this hypothesis, we exposed p53-proficient and p53-deficient cells to strong p53 activators, and either to IFNα or IFNγ. Subsequently, we estimated the phosphorylation status of STAT1 and the expression of genes regulated by either of these cytokines. Strong activation of p53 reduced the phosphorylation of STAT1 on Tyr701, however surprisingly it did not lead to reduced expression of most tested interferon-stimulated genes. On contrary, p53 and IFNγ synergized in the activation of CASP1, IFIT1 and IFIT3 genes. We conclude that the interactions between p53 and interferon-activated pathways are more complicated than initially expected, but the apparent cooperation between p53 and IFNγ deserves further studies.
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
