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Perilipin 1 binds to aquaporin 7 in human adipocytes and controls its mobility via protein kinase A mediated phosphorylation

Söndergaard Hansen, Jesper LU ; Krintel, Christian LU ; Hernebring, Malin; Haataja, Tatu J K LU ; de Marè, Sofia LU ; Wasserstrom, Sebastian LU ; Kosinska-Eriksson, Urszula; Palmgren, Madelene; Holm, Cecilia LU and Stenkula, Karin G. LU , et al. (2016) In Metabolism, Clinical and Experimental 65(12). p.1731-1742
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... (More)

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.

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@article{dffff6bf-ec34-493e-9c3a-b99ebe2aa117,
  abstract     = {<p>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.</p>},
  author       = {Söndergaard Hansen, Jesper and Krintel, Christian and Hernebring, Malin and Haataja, Tatu J K and de Marè, Sofia and Wasserstrom, Sebastian and Kosinska-Eriksson, Urszula and Palmgren, Madelene and Holm, Cecilia and Stenkula, Karin G. and Jones, Helena A. and Lindkvist-Petersson, Karin},
  issn         = {0026-0495},
  keyword      = {Adipocyte,Aquaporin 7,Glycerol,Perilipin 1,PKA},
  language     = {eng},
  month        = {12},
  number       = {12},
  pages        = {1731--1742},
  publisher    = {Elsevier},
  series       = {Metabolism, Clinical and Experimental},
  title        = {Perilipin 1 binds to aquaporin 7 in human adipocytes and controls its mobility via protein kinase A mediated phosphorylation},
  url          = {http://dx.doi.org/10.1016/j.metabol.2016.09.004},
  volume       = {65},
  year         = {2016},
}