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Florentina Negoita

Visiting research fellow

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EHD2 regulates adipocyte function and is enriched at cell surface-associated lipid droplets in primary human adipocytes

Author

  • Björn Morén
  • Björn Hansson
  • Florentina Negoita
  • Claes Fryklund
  • Richard Lundmark
  • Olga Göransson
  • Karin G. Stenkula

Summary, in English

Adipocytes play a central role in energy balance, and dysfunctional adipose tissue severely affects systemic energy homeostasis. The ATPase EH domain-containing 2 (EHD2) has previously been shown to regulate caveolae, plasma membrane-specific domains that are involved in lipid uptake and signal transduction. Here, we investigated the role of EHD2 in adipocyte function. We demonstrate that EHD2 protein expression is highly up-regulated at the onset of triglyceride accumulation during adipocyte differentiation. Small interfering RNA-mediated EHD2 silencing affected the differentiation process and impaired insulin sensitivity, lipid storage capacity, and lipolysis. Fluorescence imaging revealed localization of EHD2 to caveolae, close to cell surface-associated lipid droplets in primary human adipocytes. These lipid droplets stained positive for glycerol transporter aquaporin 7 and phosphorylated perilipin-1 following adrenergic stimulation. Further, EHD2 overexpression in human adipocytes increased the lipolytic signaling and suppressed the activity of transcription factor PPARγ. Overall, these data suggest that EHD2 plays a key role for adipocyte function.

Department/s

  • Glucose Transport and Protein Trafficking
  • EXODIAB: Excellence in Diabetes Research in Sweden
  • Protein Phosphorylation

Publishing year

2019

Language

English

Pages

1147-1159

Publication/Series

Molecular Biology of the Cell

Volume

30

Issue

10

Document type

Journal article

Publisher

American Society for Cell Biology

Topic

  • Cell and Molecular Biology

Status

Published

Research group

  • Glucose Transport and Protein Trafficking
  • Protein Phosphorylation

ISBN/ISSN/Other

  • ISSN: 1059-1524