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. 2016 Jan 11;6:19143. doi: 10.1038/srep19143

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In fed conditions, SF-1 sumoylation is increased by activation of the insulin-PI3K signaling pathway and promotes SF-1-mediated transcriptional regulation. Conversely, sumoylation of SF-1 acts as a degradation signal under fasted conditions. Therefore, sumoylation promotes ubiquitin-dependent degradation of SF-1 and attenuates SF-1 transcriptional activity under fasted condition.