The phosphorylation of carboxyl-terminal eIF2α by SPA kinases contributes to enhanced translation efficiency during photomorphogenesis

Hui-Hsien Chang, Lin-Chen Huang, Karen S. Browning, Enamul Huq and Mei-Chun Cheng ()
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Hui-Hsien Chang: National Taiwan University
Lin-Chen Huang: National Taiwan University
Karen S. Browning: University of Texas at Austin
Enamul Huq: University of Texas at Austin
Mei-Chun Cheng: National Taiwan University

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract Light triggers an enhancement of global translation during photomorphogenesis in Arabidopsis, but little is known about the underlying mechanisms. The phosphorylation of the α-subunit of eukaryotic initiation factor 2 (eIF2α) at a conserved serine residue in the N-terminus has been shown as an important mechanism for the regulation of protein synthesis in mammalian and yeast cells. However, whether the phosphorylation of this residue in plant eIF2α plays a role in regulation of translation remains elusive. Here, we show that the quadruple mutant of SUPPRESSOR OF PHYA-105 family members (SPA1-SPA4) display repressed translation efficiency after light illumination. Moreover, SPA1 directly phosphorylates the eIF2α C-terminus under light conditions. The C-term-phosphorylated eIF2α promotes translation efficiency and photomorphogenesis, whereas the C-term-unphosphorylated eIF2α results in a decreased translation efficiency. We also demonstrate that the phosphorylated eIF2α enhances ternary complex assembly by promoting its affinity to eIF2β and eIF2γ. This study reveals a unique mechanism by which light promotes translation via SPA1-mediated phosphorylation of the C-terminus of eIF2α in plants.

Date: 2024
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DOI: 10.1038/s41467-024-47848-7

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