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

Research output: Contribution to journalArticle

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.

Details

Authors
Organisations
External organisations
  • University of Gothenburg
  • Lund University
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Cell and Molecular Biology

Keywords

  • Adipocyte, Aquaporin 7, Glycerol, Perilipin 1, PKA
Original languageEnglish
Pages (from-to)1731-1742
Number of pages12
JournalMetabolism, Clinical and Experimental
Volume65
Issue number12
StatePublished - 2016 Dec 1
Peer-reviewedYes