Cited by 298PI3K/AKT/mTOR signaling in cancerRNA and protein synthesis mechanismsMetabolism, Diabetes, and Cancer

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Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase‐3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin

Welsh, Gavin I, Miller, Christa M, Loughlin, A.Jane, Price, Nigel T·1998·FEBS Letters

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Abstract

Eukaryotic initiation factor eIF2B catalyses a key regulatory step in mRNA translation. eIF2B and total protein synthesis are acutely activated by insulin, and this requires phosphatidylinositol 3‐kinase (PI 3‐kinase). The ϵ‐subunit of eIF2B is phosphorylated by glycogen synthase kinase‐3 (GSK‐3), which is inactivated by insulin in a PI 3‐kinase‐dependent manner. Here we identify the phosphorylation site in eIF2Bϵ as Ser 540 and show that treatment of eIF2B with GSK‐3 inhibits its activity. Ser 540 is phosphorylated in intact cells and undergoes dephosphorylation in response to insulin. This is blocked by PI 3‐kinase inhibitors. Insulin‐induced dephosphorylation of this inhibitory site in eIF2B seems likely to be important in the overall activation of translation by this hormone.

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Authors: Welsh, G. I., Miller, C. M., Loughlin, A. J., & Price, N. T.
Affiliations: University of Kent (GB)
University of Bristol (GB)
ORCID: Welsh, Gavin I
Venue: FEBS Letters
Publisher: Wiley
Published: 1998-01-09
Volume: 421
Issue: 2
Pages: 125-130
ISSN: 0014-5793 (ISSN-L)
1873-3468
DOI: 10.1016/s0014-5793(97)01548-2
OpenAlex: W2057327606
Cited by: 298
References: 39
Citations by year: 2026: 2 · 2025: 3 · 2024: 3 · 2023: 4 · 2022: 6 · 2021: 7 · 2020: 9 · 2019: 5 · 2018: 17 · 2017: 7 · 2016: 8 · 2015: 9 · 2014: 7 · 2013: 16 · 2012: 19
FWCI: 5.23
Type: journal article
Language: en
Open access: closed
Licence: onlinelibrary.wiley.com/termsAndConditions#vor (vor, 32 d)
Locations: FEBS Letters (publishedVersion)
PubMed (publishedVersion)
Kent Academic Repository (University of Kent) (submittedVersion)
Open Research Online (The Open University) (submittedVersion)
Funders: Wellcome Trust
Topics: 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 and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: eIF2B, glycogen synthase kinase-3, dephosphorylation, insulin signaling, phosphatidylinositol 3-kinase, mRNA translation regulation, protein synthesis
MeSH terms: Amino Acid Sequence, Animals, Binding Sites, Cricetinae, Insulin, Molecular Sequence Data, Phosphorylation, Rabbits, Serine, Eukaryotic Initiation Factor-2, CHO Cells, Conserved Sequence, Calcium-Calmodulin-Dependent Protein Kinases, Glycogen Synthase Kinases, Glycogen Synthase Kinase 3

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Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase‐3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin

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