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Regulation of Eukaryotic Initiation Factor eIF2B

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Signaling Pathways for Translation

Part of the book series: Progress in Molecular and Subcellular Biology ((PMSB,volume 26))

Abstract

The initiation of mRNA translation requires the recruitment to the ribosome of the initiator methionyl-tRNA (Met-tRNAi). This is mediated by initiation factor-2 (eIF2), a heterotrimeric protein of subunits α-γ, of which the γ binds guanine nucleotides (Fig. 1). eIF2 can only interact with Met-tRNAi when it is in its GTP-bound form. The GTP molecule is hydrolysed late in the initiation process and eIF2 is released from the ribosome as a complex with GDP, which is inactive in binding Met-tRNAi. To enable eIF2 to participate further in translation initiation, the GDP must be released and replaced by GTP, a process termed guanine nucleotide exchange. The off-rate of GDP bound to eIF2 is very slow, and a protein factor (a guanine nucleotide exchange factor) is required to accelerate this process and facilitate the regeneration of active eIF2-GTP for subsequent rounds of translation initiation. This guanine nucleotide exchange factor is eIF2B (Fig. 1.)

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  1. Department of Anatomy and Physiology, MSI/WTB Complex, University of Dundee, Dow Street, Dundee, DD1 5EH, UK

    Christopher G. Proud

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  1. Christopher G. Proud
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  1. Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA, 71130, USA

    Robert E. Rhoads

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© 2001 Springer-Verlag Berlin Heidelberg

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Proud, C.G. (2001). Regulation of Eukaryotic Initiation Factor eIF2B. In: Rhoads, R.E. (eds) Signaling Pathways for Translation. Progress in Molecular and Subcellular Biology, vol 26. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56688-2_4

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  • DOI: https://doi.org/10.1007/978-3-642-56688-2_4

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