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

Zhiqi Sun, Jingyi Gong, Han Wu, Wenyi Xu, Lizhen Wu, Dijin Xu, Jinlan Gao, Jia-wei Wu, Hongyuan Yang, Maojun Yang and Peng Li ()
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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
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
Jia-wei Wu: Tsinghua-Peking Center for 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
Peng Li: Tsinghua-Peking Center for Life Sciences, Tsinghua University

Nature Communications, 2013, vol. 4, issue 1, 1-15

Abstract: 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.

Date: 2013
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DOI: 10.1038/ncomms2581

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