An evolutionarily conserved interaction of tumor suppressor protein Pdcd4 with the poly(A)-binding protein contributes to translation suppression by Pdcd4
Open accessAbstract
The tumor suppressor protein programmed cell death 4 (Pdcd4) has been implicated in the translational regulation of specific mRNAs, however, the identities of the natural Pdcd4 target mRNAs and the mechanisms by which Pdcd4 affects their translation are not well understood. Pdcd4 binds to the eukaryotic translation initiation factor eIF4A and inhibits its helicase activity, which has suggested that Pdcd4 suppresses translation initiation of mRNAs containing structured 5'-untranslated regions. Recent work has revealed a second inhibitory mechanism, which is eIF4A-independent and involves direct RNA-binding of Pdcd4 to the target mRNAs. We have now identified the poly(A)-binding protein (PABP) as a novel direct interaction partner of Pdcd4. The ability to interact with PABP is shared between human and Drosophila Pdcd4, indicating that it has been highly conserved during evolution. Mutants of Pdcd4 that have lost the ability to interact with PABP fail to stably associate with ribosomal complexes in sucrose density gradients and to suppress translation, as exemplified by c-myb mRNA. Overall, our work identifies PABP as a novel functionally relevant Pdcd4 interaction partner that contributes to the regulation of translation by Pdcd4.
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PDCD4 protein is a binding partner of the poly(A) binding protein (PABP).
“Further, PDCD4-protein is a binding partner of the poly (A) binding protein (PABP) that binds to the poly A tail of mRNA and control protein synthesis interacting with the translation initiation complex [31].”
From Control Mechanisms of the Tumor Suppressor PDCD4: Expression and Functions (2019) · cites this paper as [31]
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- Authors
- Fehler, O., Singh, P., Haas, A., Ulrich, D., Müller, J. P., Ohnheiser, J., & Klempnauer, K.-H.
- Affiliations
- University of Münster (DE)
- Corresponding author
- Klempnauer, Karl-Heinz
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2014-09-04
- Volume
- 42
- Issue
- 17
- Pages
- 11107-11118
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC4176178
- OpenAlex
- W2069932990
- Cited by
- 35
- References
- 50
- Citations by year
- 2026: 6 · 2025: 2 · 2024: 3 · 2021: 2 · 2020: 5 · 2019: 1 · 2018: 4 · 2017: 3 · 2016: 5 · 2015: 3
- FWCI
- 1.50
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nucleic Acids Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Deutsche Krebshilfe (109269)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Keywords
- PDCD4, poly(A)-binding protein, protein synthesis inhibition, protein-protein interaction, ribosome association, 5' untranslated region, Drosophila, tumor suppressor
- MeSH terms
- Animals, Humans, Mutation, Ribosomes, RNA, Protein Biosynthesis, RNA-Binding Proteins, Evolution, Molecular, Proto-Oncogene Proteins c-myb, Tumor Suppressor Proteins, Drosophila Proteins, Poly(A)-Binding Proteins, Apoptosis Regulatory Proteins, Protein Interaction Domains and Motifs
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