Perilipin 1 binds to aquaporin 7 in human adipocytes and controls its mobility via protein kinase A mediated phosphorylation.
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Hansen JS, Krintel C, Hernebring M, Haataja TJ, de Mare S, Wasserstrom S, Kosinska-Eriksson U, Palmgren M, Holm C, Stenkula KG, Jones HA, Lindkvist-Petersson K
Perilipin 1 binds to aquaporin 7 in human adipocytes and controls its mobility via protein kinase A mediated phosphorylation.
Metabolism. 2016 Dec;65(12):1731-1742. doi: 10.1016/j.metabol.2016.09.004. Epub 2016 Sep 22.
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- 27832861 [ View in PubMed]
- Abstract
Accumulating evidence suggests that dysregulated glycerol metabolism contributes to the pathophysiology of obesity and type 2 diabetes. Glycerol efflux from adipocytes is regulated by the aquaglyceroporin AQP7, which is translocated upon hormone stimulation. Here, we propose a molecular mechanism where the AQP7 mobility in adipocytes is dependent on perilipin 1 and protein kinase A. Biochemical analyses combined with ex vivo studies in human primary adipocytes, demonstrate that perilipin 1 binds to AQP7, and that catecholamine activated protein kinase A phosphorylates the N-terminus of AQP7, thereby reducing complex formation. Together, these findings are indicative of how glycerol release is controlled in adipocytes, and may pave the way for the future design of drugs against human metabolic pathologies.