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Sumoylation of eIF4A2 affects stress granule formation

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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 Watts
Regulation 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.

History

Publication status

  • Published

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  • Published version

Journal

Journal of Cell Science

ISSN

0021-9533

Publisher

Company of Biologists

Issue

12

Volume

129

Page range

2407-2415

Department affiliated with

  • Biochemistry Publications

Full text available

  • Yes

Peer reviewed?

  • Yes

Legacy Posted Date

2016-05-13

First Open Access (FOA) Date

2017-03-02

First Compliant Deposit (FCD) Date

2016-05-13

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