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Sumoylation of eIF4A2 affects stress granule formation
Version 2 2023-06-12, 06:39
Version 1 2023-06-09, 01:13
journal contribution
posted on 2023-06-12, 06:39 authored by Jirapas Jongjitwimol, Robert A Baldock, Simon Morley, Felicity WattsRegulation of protein synthesis is crucial for cells to maintain viability and to prevent unscheduled proliferation that could lead to tumorigenesis. Exposure to stress results in stalling of translation, with many translation initiation factors, ribosomal subunits and mRNAs being sequestered into stress granules or P bodies. This allows the re-programming of the translation machinery. Many aspects of translation are regulated by post-translational modification. Several proteomic screens have identified translation initiation factors as targets for sumoylation, although in many cases the role of this modification has not been determined. We show here that eIF4A2 is modified by SUMO, with sumoylation occurring on a single residue (K226). We demonstrate that sumoylation of eIF4A2 is modestly increased in response to arsenite and ionising radiation but decreases in response to heat shock or hippuristanol. In arsenite treated cells but not in hippuristanol treated cells, eIF4A2 is recruited to stress granules, suggesting sumoylation of eIF4A2 correlates with its recruitment to stress granules. Furthermore, we demonstrate that inability to sumoylate eIF4A2 results in impaired stress granule formation, indicating a novel role for sumoylation in the stress response.
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- Published
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- Published version
Journal
Journal of Cell ScienceISSN
0021-9533Publisher
Company of BiologistsExternal DOI
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12Volume
129Page range
2407-2415Department affiliated with
- Biochemistry Publications
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- Yes
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- Yes
Legacy Posted Date
2016-05-13First Open Access (FOA) Date
2017-03-02First Compliant Deposit (FCD) Date
2016-05-13Usage metrics
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