What is it about?

eIF4G has a key role in the initiation of proein synthesis. It acts as a scaffold protein and interacts with a number of other key initiation factors. We demonstrate here that in response to stress, eIF4G can be modified by a small protein modifier (SUMO). This modification occurs in domains known to be involved in specific protein-protein ineractions, thus the modification by SUMO may affect interactions of eIF4G with other proteins.

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Why is it important?

Cells expend a large amount of energy synthesising proteins, thus regulation of translation, particularly under stress conditions is is important for cells to maintain viability. Sumoylation is likely to be a key regulator of translation under stress conditions e.g. in response to heat stress

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This page is a summary of: The S. pombe Translation Initiation Factor eIF4G Is Sumoylated and Associates with the SUMO Protease Ulp2, PLoS ONE, May 2014, PLOS,
DOI: 10.1371/journal.pone.0094182.
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