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Perilipin1 promotes unilocular lipid droplet formation through the activation of Fsp27 in adipocytes

Author

Listed:
  • Zhiqi Sun

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University)

  • Jingyi Gong

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University)

  • Han Wu

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University
    Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Wenyi Xu

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University)

  • Lizhen Wu

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University)

  • Dijin Xu

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University)

  • Jinlan Gao

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University
    Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Jia-wei Wu

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University
    MOE Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University)

  • Hongyuan Yang

    (School of Biotechnology and Biomolecular Sciences, the University of New South Wales)

  • Maojun Yang

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University
    Center for Structural Biology, School of Life Sciences, Tsinghua University)

  • Peng Li

    (Tsinghua-Peking Center for Life Sciences, Tsinghua University)

Abstract

Mature white adipocytes contain a characteristic unilocular lipid droplet. However, the molecular mechanisms underlying unilocular lipid droplet formation are poorly understood. We previously showed that Fsp27, an adipocyte-specific lipid droplet-associated protein, promotes lipid droplet growth by initiating lipid exchange and transfer. Here, we identify Perilipin1 (Plin1), another adipocyte-specific lipid droplet-associated protein, as an Fsp27 activator. Plin1 interacts with the CIDE-N domain of Fsp27 and markedly increases Fsp27-mediated lipid exchange, lipid transfer and lipid droplet growth. Functional cooperation between Plin1 and Fsp27 is required for efficient lipid droplet growth in adipocytes, as depletion of either protein impairs lipid droplet growth. The CIDE-N domain of Fsp27 forms homodimers and disruption of CIDE-N homodimerization abolishes Fsp27-mediated lipid exchange and transfer. Interestingly, Plin1 can restore the activity of CIDE-N homodimerization-defective mutants of Fsp27. We thus uncover a novel mechanism underlying lipid droplet growth and unilocular lipid droplet formation that involves the cooperative action of Fsp27 and Plin1 in adipocytes.

Suggested Citation

  • Zhiqi Sun & Jingyi Gong & Han Wu & Wenyi Xu & Lizhen Wu & Dijin Xu & Jinlan Gao & Jia-wei Wu & Hongyuan Yang & Maojun Yang & Peng Li, 2013. "Perilipin1 promotes unilocular lipid droplet formation through the activation of Fsp27 in adipocytes," Nature Communications, Nature, vol. 4(1), pages 1-15, June.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms2581
    DOI: 10.1038/ncomms2581
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    Cited by:

    1. Shao-Chin Wu & Yuan-Ming Lo & Jui-Hao Lee & Chin-Yau Chen & Tung-Wei Chen & Hong-Wen Liu & Wei-Nan Lian & Kate Hua & Chen-Chung Liao & Wei-Ju Lin & Chih-Yung Yang & Chien-Yi Tung & Chi-Hung Lin, 2022. "Stomatin modulates adipogenesis through the ERK pathway and regulates fatty acid uptake and lipid droplet growth," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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