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. 2012 Dec 21;14(1):177–190. doi: 10.3390/ijms14010177

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© 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

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Regulation of eIF2 activity. The guanine nucleotide-exchange activity of eIF2B permits the association of the eIF2γ subunit of eIF2 with GTP. This is a prerequisite for the formation of the ternary eIF2.GTP.Met.tRNAi complex. eIF2 and eIF2B activities are inhibited by phosphorylation of their eIF2α (by HRI, PKR, PERK or GCN2) and eIF2Bɛ (by GSK3β) subunits. eIF2B activity is also indirectly inhibited (sequestered by eIF2γ) as a consequence of eIF2α phosphorylation. See text for details.