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AMPK regulates K(ATP) channel trafficking via PTEN inhibition in leptin-treated pancreatic ß-cells.

Authors: Park, Sun-Hyun  Ho, Won-Kyung  Jeon, Ju-Hong 
Citation: Park SH, etal., Biochem Biophys Res Commun. 2013 Nov 1;440(4):539-44. doi: 10.1016/j.bbrc.2013.09.099. Epub 2013 Oct 5.
Pubmed: (View Article at PubMed) PMID:24103758
DOI: Full-text: DOI:10.1016/j.bbrc.2013.09.099

Leptin regulates pancreatic ß-cell excitability through AMP-activated protein kinase (AMPK)-mediated ATP-sensitive potassium (KATP) channel trafficking. However, the signaling components connecting AMPK to KATP channel trafficking are not identified. In this study, we discovered that AMPK inhibits phosphatase and tensin homologue (PTEN) via glycogen synthase kinase 3ß (GSK3ß) and this signaling pathway is crucial for KATP channel trafficking in leptin-treated pancreatic ß-cells. Pharmacologic or genetic inhibition of AMPK or GSK3ß, but not casein kinase 2 (CK2), impaired leptin-induced PTEN inactivation and thereby KATP channel trafficking. The PTEN mutant lacking both protein and lipid phosphatase activity is sufficient to induce KATP channel trafficking without leptin. These results present a novel signaling mechanism that underlies leptin regulation of KATP channel trafficking in pancreatic ß-cells. Our findings assist in gaining a broader perspective on the peripheral action of leptin on pancreatic ß-cell physiology and glucose homeostasis.

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RGD Object Information
RGD ID: 12802338
Created: 2017-04-05
Species: All species
Last Modified: 2017-04-05
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.