PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains
Open accessAbstract
Programmed Cell Death 4 (PDCD4) is a protein known to bind eukaryotic initiation factor 4A (eIF4A), inhibit translation initiation, and act as a tumor suppressor. PDCD4 contains two C-terminal MA3 domains, which are thought to be responsible for its inhibitory function. Here, we analyze the structures and inhibitory functions of these two PDCD4 MA3 domains by x-ray crystallography, NMR, and surface plasmon resonance. We show that both MA3 domains are structurally and functionally very similar and bind specifically to the eIF4A N-terminal domain (eIF4A-NTD) using similar binding interfaces. We found that the PDCD4 MA3 domains compete with the eIF4G MA3 domain and RNA for eIF4A binding. Our data provide evidence that PDCD4 inhibits translation initiation by displacing eIF4G and RNA from eIF4A. The PDCD4 MA3 domains act synergistically to form a tighter and more stable complex with eIF4A, which explains the need for two tandem MA3 domains.
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Levels of the translation repressor PDCD4 are significantly reduced in Tex cells both in vitro and in vivo.
“Fourth, levels of the translation repressor PDCD4 (refs. 36,37) were significantly reduced in Tex cells both in vitro and in vivo”
From Proteotoxic stress response drives T cell exhaustion and immune evasion (2025) · cites this paper as [36]
MA-3 domains of PDCD4 are homologous to the MA-3 domain of eIF4G and compete with it for eIF4A binding.
“MA-3 domains of PDCD4 are homologous to the MA-3 domain of eIF4G and compete with it for eIF4A binding39,40.”
From PDCD4 triggers α-synuclein accumulation and motor deficits via co-suppressing TFE3 and TFEB translation in a model of Parkinson’s disease (2024) · cites this paper as [39]
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- Authors
- Suzuki, C., Garces, R. G., Edmonds, K. A., Hiller, S., Hyberts, S. G., Marintchev, A., & Wagner, G.
- Affiliations
- Harvard University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-03-04
- Volume
- 105
- Issue
- 9
- Pages
- 3274-3279
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2265113
- OpenAlex
- W2079859240
- Cited by
- 165
- References
- 21
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 15 · 2023: 5 · 2022: 4 · 2021: 8 · 2020: 10 · 2019: 8 · 2018: 5 · 2017: 5 · 2016: 4 · 2015: 9 · 2014: 15 · 2013: 14 · 2012: 12
- FWCI
- 4.39
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Energy (DE‐ AC02‐06CH11357, AC02‐06CH11357, contract DE-AC02-06CH11357, 06CH11357, RR-15301, DE-AC02-)
- National Institutes of Health (DE-AC02–06CH11357, GM47467, RR15301)
- National Cancer Institute (DE-AC02-06CH11357, CA68262, K01CA119107, R01CA068262)
- National Institute of General Medical Sciences (GM47467, P01GM047467)
- National Center for Research Resources (RR 15301, P41RR015301)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- PDCD4, eIF4A, translation initiation inhibition, eIF4G, protein-protein binding, tumor suppressor, protein complex stability
- MeSH terms
- Binding, Competitive, Humans, Protein Binding, RNA, Protein Biosynthesis, RNA-Binding Proteins, Protein Structure, Tertiary, Crystallography, X-Ray, Eukaryotic Initiation Factor-4A, Eukaryotic Initiation Factor-4G, Apoptosis Regulatory Proteins
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