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The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro

Cuddihy, Andrew R, Hoi-Tao Wong, Andrew, Wai Ning Tam, Nancy, Li, Suiyang, Koromilas, Antonis E·1999·Oncogene

DOI 10.1038/sj.onc.1202620

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Abstract

The tumor suppressor p53 is a multifunctional protein that plays a critical role in modulating cellular responses upon DNA damage or other stresses. These functions of p53 are regulated both by protein-protein interactions and phosphorylation. The double-stranded RNA activated protein kinase PKR is a serine/threonine kinase that modulates protein synthesis through the phosphorylation of translation initiation factor eIF-2alpha. PKR is an interferon (IFN)-inducible protein that is thought to mediate the anti-viral and anti-proliferative effects of IFN via its capacity to inhibit protein synthesis. Here we report that PKR physically associates with p53. The interaction of PKR with p53 is enhanced by IFNs and upon conditions that p53 acquires a wild type conformation. PKR/p53 complex formation in vitro requires the N-terminal regulatory domain of PKR and the last 30 amino acids of the C-terminus of human p53. In addition, p53 may function as a substrate of PKR since phosphorylation of human p53 on serine392 is induced by activated PKR in vitro. These novel findings raise the possibility of a functional interaction between PKR and p53 in vivo, which may account, at least in part, for the ability of each protein to regulate gene expression at both the transcriptional and the translational levels.

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Authors: Cuddihy, A. R., Hoi-Tao Wong, A., Wai Ning Tam, N., Li, S., & Koromilas, A. E.
Affiliations: McGill University (CA)
ORCID: Cuddihy, Andrew R
Koromilas, Antonis E
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 1999-04-28
Volume: 18
Issue: 17
Pages: 2690-2702
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1202620
OpenAlex: W2010358674
Cited by: 203
References: 68
Citations by year: 2026: 2 · 2024: 4 · 2023: 10 · 2022: 4 · 2021: 6 · 2020: 5 · 2019: 6 · 2018: 5 · 2017: 4 · 2016: 5 · 2015: 2 · 2014: 5 · 2013: 7 · 2012: 5
FWCI: 6.76
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Keywords: PKR, p53, protein-protein interaction, double-stranded RNA-dependent protein kinase, interferon, tumor suppressor, N-terminal regulatory domain, eIF2α, protein synthesis inhibition, gene expression regulation
MeSH terms: Amino Acid Sequence, Animals, Cell Line, Humans, Molecular Sequence Data, Phosphorylation, Precipitin Tests, RNA, Double-Stranded, Serine, Tumor Suppressor Protein p53, Protein Structure, Tertiary, eIF-2 Kinase

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The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro

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