Structural basis for the inhibition of translation through eIF2α phosphorylation
Author:
Funder
Wellcome Trust
Medical Research Council
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/s41467-019-10606-1.pdf
Reference84 articles.
1. Das, S., Ghosh, R. & Maitra, U. Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein. J. Biol. Chem. 276, 6720–6726 (2001).
2. Paulin, F. E., Campbell, L. E., O’Brien, K., Loughlin, J. & Proud, C. G. Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein. Curr. Biol. 11, 55–59 (2001).
3. Algire, M. A., Maag, D. & Lorsch, J. R. Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol. Cell 20, 251–262 (2005).
4. Majumdar, R. & Maitra, U. Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation. EMBO J. 24, 3737–3746 (2005).
5. Llácer, J. L. et al. Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition. Elife 7, e39273 (2018).
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