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PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains

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Suzuki, Chikako, Garces, Robert G., Edmonds, Katherine A., Hiller, Sebastian, Hyberts, Sven G., Marintchev, Assen, Wagner, Gerhard·2008·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.0712235105PMC PMC2265113

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Abstract

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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Authors: Suzuki, C., Garces, R. G., Edmonds, K. A., Hiller, S., Hyberts, S. G., Marintchev, A., & Wagner, G.
Affiliations: Harvard University (US)
ORCID: Edmonds, Katherine A.
Hiller, Sebastian
Hyberts, Sven G.
Marintchev, Assen
Wagner, Gerhard
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
DOI: 10.1073/pnas.0712235105
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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PDCD4 inhibits translation initiation by binding to eIF4A using both its MA3 domains

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