mRNA helicases: the tacticians of translational control
Open accessAbstract
The translation initiation step in eukaryotes is highly regulated and rate-limiting. During this process, the 40S ribosomal subunit is usually recruited to the 5' terminus of the mRNA. It then migrates towards the initiation codon, where it is joined by the 60S ribosomal subunit to form the 80S initiation complex. Secondary structures in the 5' untranslated region (UTR) can impede binding and movement of the 40S ribosome. The canonical eukaryotic translation initiation factor eIF4A (also known as DDX2), together with its accessory proteins eIF4B and eIF4H, is thought to act as a helicase that unwinds secondary structures in the mRNA 5' UTR. Growing evidence suggests that other helicases are also important for translation initiation and may promote the scanning processivity of the 40S subunit, synergize with eIF4A to 'melt' secondary structures or facilitate translation of a subset of mRNAs.
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mTOR and MAPK signaling converge to regulate protein synthesis through the eIF4F translation initiation complex, composed of eIF4A, eIF4E, and eIF4G.
“Signaling via mTOR and MAPK converge to regulate protein synthesis through the eIF4F translation initiation complex, composed of the DEAD-box RNA helicases eIF4A, the cap binding protein eIF4E, and the regulatory scaffold protein eIF4G (14).”
From Targeting eIF4A-dependent translation in genetically complex sarcoma (2026) · cites this paper as [14]
IMP2 directly binds to the eIF4A protein, a member of the eIF4F translation initiation complex that acts as the helicase responsible for unwinding RNA secondary and tertiary structures to allow the ribosome to more efficiently translate mRNA into protein.
“IMP2 directly binds to the eIF4A protein, a member of the eIF4F translation initiation complex that acts as the helicase responsible for unwinding RNA secondary and tertiary structures to allow the ribosome to more efficiently translate mRNA into protein [33,34].”
From IMPlications of IMP2 in RNA Biology and Disease (2025) · cites this paper as [34]
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References 129 · Cited by 323
- Authors
- Parsyan, A., Svitkin, Y., Shahbazian, D., Gkogkas, C., Lasko, P., Merrick, W. C., & Sonenberg, N.
- Affiliations
- McGill University (CA)
- Yale University (US)
- Case Western Reserve University (US)
- Corresponding author
- Sonenberg, Nahum
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2011-03-23
- Volume
- 12
- Issue
- 4
- Pages
- 235-245
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2086079901
- Cited by
- 323
- References
- 129
- Citations by year
- 2026: 16 · 2025: 9 · 2024: 11 · 2023: 15 · 2022: 16 · 2021: 15 · 2020: 18 · 2019: 14 · 2018: 25 · 2017: 18 · 2016: 28 · 2015: 27 · 2014: 35 · 2013: 26 · 2012: 39
- FWCI
- 3.25
- Type
- journal article
- Language
- en
- Open access
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@McGill (McGill) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- Canadian Institutes of Health Research
- 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
- translation initiation, eIF4A, eIF4B, eIF4H, 5' untranslated region, mRNA secondary structure, processivity, eIF4G, translation initiation factors
- MeSH terms
- Animals, Humans, Models, Genetic, RNA, Messenger, Protein Biosynthesis, Codon, Initiator, RNA Helicases, Eukaryotic Initiation Factor-4A, Eukaryotic Initiation Factors
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