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We have identified Serine 73 as a novel GSK-3β site on SREBP-1c that alters its affinity for SCAP, and proteasomal degradation. Phosphorylation of Serine 73 by GSK-3β during starvation (insulin-depleted stat) may lead to lower levels of SREBP-1c; conversely, de-phosphorylation of this site may be involved in stabilizing SREBP-1c by insulin (by blocking GSK-3β action). A functional role of this site needs to be corroborated  in vivo .

bioscience reports

Glycogen synthase kinase-3-mediated phosphorylation of serine 73 targets sterol response element binding protein-1c (SREBP-1c) for proteasomal degradation