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Enrichment of hydroxylated C24- and C26-acyl-chain sphingolipids mediates PIN2 apical sorting at trans-Golgi network subdomains

Author

Listed:
  • Valérie Wattelet-Boyer

    (UMR 5200 Membrane Biogenesis Laboratory, CNRS-University of Bordeaux)

  • Lysiane Brocard

    (Bordeaux Imaging Center, UMS 3420 CNRS, US4 INSERM, University of Bordeaux)

  • Kristoffer Jonsson

    (Umeå Plant Science Centre, Swedish University for Agricultural Sciences)

  • Nicolas Esnay

    (UMR 5200 Membrane Biogenesis Laboratory, CNRS-University of Bordeaux)

  • Jérôme Joubès

    (UMR 5200 Membrane Biogenesis Laboratory, CNRS-University of Bordeaux)

  • Frédéric Domergue

    (UMR 5200 Membrane Biogenesis Laboratory, CNRS-University of Bordeaux)

  • Sébastien Mongrand

    (UMR 5200 Membrane Biogenesis Laboratory, CNRS-University of Bordeaux)

  • Natasha Raikhel

    (Center for Plant Cell Biology, University of California)

  • Rishikesh P. Bhalerao

    (Umeå Plant Science Centre, Swedish University for Agricultural Sciences
    College of Science, KSU)

  • Patrick Moreau

    (UMR 5200 Membrane Biogenesis Laboratory, CNRS-University of Bordeaux
    Bordeaux Imaging Center, UMS 3420 CNRS, US4 INSERM, University of Bordeaux)

  • Yohann Boutté

    (UMR 5200 Membrane Biogenesis Laboratory, CNRS-University of Bordeaux)

Abstract

The post-Golgi compartment trans-Golgi Network (TGN) is a central hub divided into multiple subdomains hosting distinct trafficking pathways, including polar delivery to apical membrane. Lipids such as sphingolipids and sterols have been implicated in polar trafficking from the TGN but the underlying mechanisms linking lipid composition to functional polar sorting at TGN subdomains remain unknown. Here we demonstrate that sphingolipids with α-hydroxylated acyl-chains of at least 24 carbon atoms are enriched in secretory vesicle subdomains of the TGN and are critical for de novo polar secretory sorting of the auxin carrier PIN2 to apical membrane of Arabidopsis root epithelial cells. We show that sphingolipid acyl-chain length influences the morphology and interconnections of TGN-associated secretory vesicles. Our results uncover that the sphingolipids acyl-chain length links lipid composition of TGN subdomains with polar secretory trafficking of PIN2 to apical membrane of polarized epithelial cells.

Suggested Citation

  • Valérie Wattelet-Boyer & Lysiane Brocard & Kristoffer Jonsson & Nicolas Esnay & Jérôme Joubès & Frédéric Domergue & Sébastien Mongrand & Natasha Raikhel & Rishikesh P. Bhalerao & Patrick Moreau & Yoha, 2016. "Enrichment of hydroxylated C24- and C26-acyl-chain sphingolipids mediates PIN2 apical sorting at trans-Golgi network subdomains," Nature Communications, Nature, vol. 7(1), pages 1-15, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12788
    DOI: 10.1038/ncomms12788
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