The eukaryotic translation initiation factor (eIF) eIF2B is a key regulator of mRNA translation, being the guanine nt exchange factor (GEF) responsible for the recycling of the heterotrimeric G-protein, eIF2, which is required to allow translation initiation to occur. Unusually for a GEF, eIF2B is a multi-subunit protein, comprising five different subunits termed α through ε in order of increasing size. eIF2B is subject to tight regulation in the cell and may also serve additional functions. Here we review recent insights into the subunit organization of the mammalian eIF2B complex, gained both from structural studies of the complex and from studies of mutations of eIF2B that result in the neurological disorder leukoencephalopathy with vanishing white matter (VWM). We will also discuss recent data from yeast demonstrating a novel function of the eIF2B complex key for translational regulation.
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December 2015
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Review Article|
November 27 2015
eIF2B: recent structural and functional insights into a key regulator of translation
Noel C. Wortham;
Noel C. Wortham
1
*University of Southampton, Centre for Biological Sciences, Life Sciences Building 85, Highfield Campus, Southampton SO17 1BJ, U.K.
†Trafalgar School, London Road, Hilsea, Portsmouth, Hampshire, PO2 9RJ, U.K.
1To whom correspondence should be addressed (emailnwortham@trafalgarschool.org.uk).
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Christopher G. Proud
Christopher G. Proud
*University of Southampton, Centre for Biological Sciences, Life Sciences Building 85, Highfield Campus, Southampton SO17 1BJ, U.K.
‡South Australian Health and Medical Research Institute, North Terrace, Adelaide SA 5000, Australia
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Publisher: Portland Press Ltd
Received:
July 24 2015
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2015 Authors; published by Portland Press Limited
2015
Biochem Soc Trans (2015) 43 (6): 1234–1240.
Article history
Received:
July 24 2015
Citation
Noel C. Wortham, Christopher G. Proud; eIF2B: recent structural and functional insights into a key regulator of translation. Biochem Soc Trans 1 December 2015; 43 (6): 1234–1240. doi: https://doi.org/10.1042/BST20150164
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