Cited by 520RNA and protein synthesis mechanismsPI3K/AKT/mTOR signaling in cancerRNA Research and Splicing

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Signalling to translation: how signal transduction pathways control the protein synthetic machinery

Proud, Christopher G.·2007·Biochemical Journal

DOI 10.1042/bj20070024

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Abstract

Recent advances in our understanding of both the regulation of components of the translational machinery and the upstream signalling pathways that modulate them have provided important new insights into the mechanisms by which hormones, growth factors, nutrients and cellular energy status control protein synthesis in mammalian cells. The importance of proper control of mRNA translation is strikingly illustrated by the fact that defects in this process or its control are implicated in a number of disease states, such as cancer, tissue hypertrophy and neurodegeneration. Signalling pathways such as those involving mTOR (mammalian target of rapamycin) and mitogen-activated protein kinases modulate the phosphorylation of translation factors, the activities of the protein kinases that act upon them and the association of RNA-binding proteins with specific mRNAs. These effects contribute both to the overall control of protein synthesis (which is linked to cell growth) and to the modulation of the translation or stability of specific mRNAs. However, important questions remain about both the contributions of individual regulatory events to the control of general protein synthesis and the mechanisms by which the translation of specific mRNAs is controlled.

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Harding, H. P., Novoa, I., Zhang, Y., Zeng, H., Wek, R. C., Schapira, M., & Ron, D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00108-8 · Cited by 3,344
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Sarbassov, D. D., Ali, S. M., Sengupta, S., Sheen, J.-H., Hsu, P. P., Bagley, A. F., Markhard, A. L., & Sabatini, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.029 · Cited by 2,365
eIF4 Initiation Factors: Effectors of mRNA Recruitment to Ribosomes and Regulators of Translation
Gingras, A., Raught, B., & Sonenberg, N. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.913 · Cited by 2,103
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Absence of S6K1 protects against age- and diet-induced obesity while enhancing insulin sensitivity
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Growing roles for the mTOR pathway
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Hinnebusch, 2000, Mechanism and regulation of methionyl-tRNA binding to ribosomes, 185
Pestova, 2006, The mechanism of translation initiation in eukaryotes, 87
Dever, 2006, The eIF2α kinases, 319
Klann, 2006, Protein synthesis and translational control in synaptic plasticity and learning and memory, 485
Shantz, 1994, Regulation of ornithine decarboxylase (ODC) expression by translation initiation factor eIF-4E, FASEB J., 8, A1309

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Authors: Proud, C. G.
Affiliations: University of British Columbia (CA)
Corresponding author: Proud, Christopher G.
ORCID: Proud, Christopher G.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2007-03-26
Volume: 403
Issue: 2
Pages: 217-234
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20070024
OpenAlex: W2080451230
Cited by: 520
References: 226
Citations by year: 2026: 5 · 2025: 6 · 2024: 8 · 2023: 10 · 2022: 10 · 2021: 11 · 2020: 14 · 2019: 17 · 2018: 21 · 2017: 20 · 2016: 21 · 2015: 26 · 2014: 29 · 2013: 37 · 2012: 50
FWCI: 4.88
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Journal (publishedVersion)
PubMed (publishedVersion)
ePrints Soton (University of Southampton) (submittedVersion)
Funders: Wellcome Trust
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: translational regulation, signal transduction, protein synthesis, mTOR, mitogen-activated protein kinase, RNA-binding proteins, mRNA stability, cell growth, nutrient signaling, energy status, hormone signaling, growth factor signaling, cancer, neurodegeneration, tissue hypertrophy
MeSH terms: Animals, Humans, Protein Binding, Ribosomes, Protein Biosynthesis, Signal Transduction, RNA-Binding Proteins

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Signalling to translation: how signal transduction pathways control the protein synthetic machinery

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