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Triacylglycerols sequester monotopic membrane proteins to lipid droplets

Author

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  • Lucie Caillon

    (Laboratoire de Physique de l’École Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université de Paris)

  • Vincent Nieto

    (University of Lyon, CNRS, Molecular Microbiology and Structural Biochemistry (MMSB, UMR 5086))

  • Pauline Gehan

    (Sorbonne Universités, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolécules (LBM), 4 place Jussieu
    Département de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM))

  • Mohyeddine Omrane

    (Laboratoire de Physique de l’École Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université de Paris)

  • Nicolas Rodriguez

    (Sorbonne Universités, UPMC Univ Paris 06, Ecole Normale Supérieure, CNRS, Laboratoire des Biomolécules (LBM), 4 place Jussieu
    Département de Chimie, Ecole Normale Supérieure, PSL Research University, UPMC Univ Paris 06, CNRS, Laboratoire des Biomolécules (LBM))

  • Luca Monticelli

    (University of Lyon, CNRS, Molecular Microbiology and Structural Biochemistry (MMSB, UMR 5086))

  • Abdou Rachid Thiam

    (Laboratoire de Physique de l’École Normale Supérieure, ENS, Université PSL, CNRS, Sorbonne Université, Université de Paris)

Abstract

Triacylglycerols (TG) are synthesized at the endoplasmic reticulum (ER) bilayer and packaged into organelles called lipid droplets (LDs). LDs are covered by a single phospholipid monolayer contiguous with the ER bilayer. This connection is used by several monotopic integral membrane proteins, with hydrophobic membrane association domains (HDs), to diffuse between the organelles. However, how proteins partition between ER and LDs is not understood. Here, we employed synthetic model systems and found that HD-containing proteins strongly prefer monolayers and returning to the bilayer is unfavorable. This preference for monolayers is due to a higher affinity of HDs for TG over membrane phospholipids. Protein distribution is regulated by PC/PE ratio via alterations in monolayer packing and HD-TG interaction. Thus, HD-containing proteins appear to non-specifically accumulate to the LD surface. In cells, protein editing mechanisms at the ER membrane would be necessary to prevent unspecific relocation of HD-containing proteins to LDs.

Suggested Citation

  • Lucie Caillon & Vincent Nieto & Pauline Gehan & Mohyeddine Omrane & Nicolas Rodriguez & Luca Monticelli & Abdou Rachid Thiam, 2020. "Triacylglycerols sequester monotopic membrane proteins to lipid droplets," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17585-8
    DOI: 10.1038/s41467-020-17585-8
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    Cited by:

    1. Yong Mi Choi & Dalila Ajjaji & Kaelin D. Fleming & Peter P. Borbat & Meredith L. Jenkins & Brandon E. Moeller & Shaveen Fernando & Surita R. Bhatia & Jack H. Freed & John E. Burke & Abdou Rachid Thiam, 2023. "Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. So-Hee Son & Gyuri Park & Junho Lim & Chang Yun Son & Seung Soo Oh & Ju Young Lee, 2022. "Chain flexibility of medicinal lipids determines their selective partitioning into lipid droplets," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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