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Role for formin-like 1-dependent acto-myosin assembly in lipid droplet dynamics and lipid storage

Author

Listed:
  • Simon G. Pfisterer

    (Faculty of Medicine, University of Helsinki
    Minerva Foundation Institute for Medical Research)

  • Gergana Gateva

    (Institute of Biotechnology, University of Helsinki)

  • Peter Horvath

    (Institute for Molecular Medicine Finland (FIMM), University of Helsinki
    Synthetic and Systems Biology Unit, Hungarian Academy of Sciences, BRC)

  • Juho Pirhonen

    (Faculty of Medicine, University of Helsinki
    Minerva Foundation Institute for Medical Research)

  • Veijo T. Salo

    (Faculty of Medicine, University of Helsinki
    Minerva Foundation Institute for Medical Research)

  • Leena Karhinen

    (Faculty of Medicine, University of Helsinki)

  • Markku Varjosalo

    (Institute of Biotechnology, University of Helsinki)

  • Samppa J. Ryhänen

    (Children’s Hospital, Helsinki University Central Hospital and University of Helsinki)

  • Pekka Lappalainen

    (Institute of Biotechnology, University of Helsinki)

  • Elina Ikonen

    (Faculty of Medicine, University of Helsinki
    Minerva Foundation Institute for Medical Research)

Abstract

Lipid droplets (LDs) are cellular organelles specialized in triacylglycerol (TG) storage undergoing homotypic clustering and fusion. In non-adipocytic cells with numerous LDs this is balanced by poorly understood droplet dissociation mechanisms. We identify non-muscle myosin IIa (NMIIa/MYH-9) and formin-like 1 (FMNL1) in the LD proteome. NMIIa and actin filaments concentrate around LDs, and form transient foci between dissociating LDs. NMIIa depletion results in decreased LD dissociations, enlarged LDs, decreased hydrolysis and increased storage of TGs. FMNL1 is required for actin assembly on LDs in vitro and for NMIIa recruitment to LDs in cells. We propose a novel acto-myosin structure regulating lipid storage: FMNL1-dependent assembly of myosin II-functionalized actin filaments on LDs facilitates their dissociation, thereby affecting LD surface-to-volume ratio and enzyme accessibility to TGs. In neutrophilic leucocytes from MYH9-related disease patients NMIIa inclusions are accompanied by increased lipid storage in droplets, suggesting that NMIIa dysfunction may contribute to lipid imbalance in man.

Suggested Citation

  • Simon G. Pfisterer & Gergana Gateva & Peter Horvath & Juho Pirhonen & Veijo T. Salo & Leena Karhinen & Markku Varjosalo & Samppa J. Ryhänen & Pekka Lappalainen & Elina Ikonen, 2017. "Role for formin-like 1-dependent acto-myosin assembly in lipid droplet dynamics and lipid storage," Nature Communications, Nature, vol. 8(1), pages 1-14, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14858
    DOI: 10.1038/ncomms14858
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