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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Resources
Starting and stopping SUMOylation What regulates the regulator?
This review summarises the latest information as to how sumoylation is regulated
SUMO modification of proteins other than transcription factors
Review on sumoylation of proteins other than transcription factors.
Cell-cycle-dependent localisation of Ulp1, a Schizosaccharomyces pombe Pmt3 (SUMO)-specific proteas
Role of another S. pombe SUMO protease
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