PTEN Modulates 5HT2C Receptor Through Its Phosphatase Activity

While PTEN is able to dephosphorylate proteins through its protein phosphastase activity (Leslie and Downes 2004), phosphorylation can occur to the intracellular loops of 5-HT2C receptor as described above. Thus, given that PTEN forms direct protein-protein interaction with 5-HT2C receptor shown above, it is plausible to hypothesize that PTEN may modulate the phosphorylation of 5-HT2C receptor through its protein phosphatase activity. To critically test this hypothesis, we prepared two types of stable PC12 cell lines. The first type of cell line demonstrated stable downregulation of PTEN after transfection of the cell line with vectors overexpressing PTEN-targeted small interfering RNA (siRNA), which results in prominently knocking down the expression of PTEN. The other cell line was transfected with wild-type PTEN constructs, which are able to overexpress PTEN. The 5-HT2C receptor agonist R06001675 induced phosphorylation in PTEN stable knockdown cells but not in wild-type PTEN-overexpressing cells

(Ji et al. 2006), suggesting that PTEN is able to dephosphorylate 5-HT2C receptor to counteract R0600175-induced phosphorylation.

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