Research ArticleMetabolism

Phosphatidylcholine Transfer Protein Interacts with Thioesterase Superfamily Member 2 to Attenuate Insulin Signaling

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Science Signaling  30 Jul 2013:
Vol. 6, Issue 286, pp. ra64
DOI: 10.1126/scisignal.2004111

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Linking Phospholipids to Insulin Signaling

Insulin promotes the uptake of glucose by the liver, skeletal muscle, and adipose tissue. Individuals with diabetes do not produce enough insulin to control their blood sugar concentrations. Thus, an understanding of the regulation of insulin signaling could provide new therapeutic avenues. Ersoy et al. found that the phospholipid-binding protein PC-TP (phosphatidylcholine transfer protein) and its interacting partner THEM2 (thioesterase superfamily member 2) attenuated insulin signaling by promoting the inhibition of two different effectors downstream of the insulin receptor. Both of these mechanisms were inhibited by a compound that prevented binding of phosphatidylcholine to PC-TP. The authors propose that PC-TP links the changes in membrane composition that occur after feeding or fasting to modulation of the activity of the insulin signaling pathway.

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