Eukaryotic translation initiation factor 4F : functional properties and physiological role
(2025) In Nucleic Acids Research 53(22).- Abstract
Successful translation requires multiple protein factors with diverse specific activities. Initiation of translation is regarded as the most tightly regulated step of this process, controlled by numerous factors. Among these is the eukaryotic initiation factor 4F (eIF4F), a protein complex composed of three subunits: the cap-binding protein eIF4E, the RNA helicase eIF4A, and the scaffolding protein eIF4G. While significant progress has been made in elucidating the structure and functions of eIF4F, several key questions remain unresolved concerning its mechanistic contributions to translational control. In this review, we discuss the roles of eIF4F in translation and its regulatory functions under diverse cellular conditions.... (More)
Successful translation requires multiple protein factors with diverse specific activities. Initiation of translation is regarded as the most tightly regulated step of this process, controlled by numerous factors. Among these is the eukaryotic initiation factor 4F (eIF4F), a protein complex composed of three subunits: the cap-binding protein eIF4E, the RNA helicase eIF4A, and the scaffolding protein eIF4G. While significant progress has been made in elucidating the structure and functions of eIF4F, several key questions remain unresolved concerning its mechanistic contributions to translational control. In this review, we discuss the roles of eIF4F in translation and its regulatory functions under diverse cellular conditions. Dysregulation of eIF4F is frequently implicated in a wide range of physiological abnormalities, confirming its critical role in the cell. We also review recent studies that position eIF4F as a global cellular regulator and expand our understanding of its role.
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- author
- Shuvalova, Ekaterina
; Al Sheikh, Walaa
; Shuvalov, Alexey
; Terenin, Ilya M.
LU
and Alkalaeva, Elena
- organization
- publishing date
- 2025-12-11
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nucleic Acids Research
- volume
- 53
- issue
- 22
- article number
- gkaf1351
- publisher
- Oxford University Press
- external identifiers
-
- pmid:41404795
- scopus:105025062318
- ISSN
- 0305-1048
- DOI
- 10.1093/nar/gkaf1351
- language
- English
- LU publication?
- yes
- additional info
- Publisher Copyright: © The Author(s) 2025. Published by Oxford University Press.
- id
- 98e27f88-cbb1-4624-a620-738c84c895cf
- date added to LUP
- 2026-02-11 15:08:10
- date last changed
- 2026-02-12 03:49:29
@article{98e27f88-cbb1-4624-a620-738c84c895cf,
abstract = {{<p>Successful translation requires multiple protein factors with diverse specific activities. Initiation of translation is regarded as the most tightly regulated step of this process, controlled by numerous factors. Among these is the eukaryotic initiation factor 4F (eIF4F), a protein complex composed of three subunits: the cap-binding protein eIF4E, the RNA helicase eIF4A, and the scaffolding protein eIF4G. While significant progress has been made in elucidating the structure and functions of eIF4F, several key questions remain unresolved concerning its mechanistic contributions to translational control. In this review, we discuss the roles of eIF4F in translation and its regulatory functions under diverse cellular conditions. Dysregulation of eIF4F is frequently implicated in a wide range of physiological abnormalities, confirming its critical role in the cell. We also review recent studies that position eIF4F as a global cellular regulator and expand our understanding of its role.</p>}},
author = {{Shuvalova, Ekaterina and Al Sheikh, Walaa and Shuvalov, Alexey and Terenin, Ilya M. and Alkalaeva, Elena}},
issn = {{0305-1048}},
language = {{eng}},
month = {{12}},
number = {{22}},
publisher = {{Oxford University Press}},
series = {{Nucleic Acids Research}},
title = {{Eukaryotic translation initiation factor 4F : functional properties and physiological role}},
url = {{http://dx.doi.org/10.1093/nar/gkaf1351}},
doi = {{10.1093/nar/gkaf1351}},
volume = {{53}},
year = {{2025}},
}