Sammanfattning

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 alpha-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.

Publicerad i

Nature Communications
2016, Volym: 7, artikelnummer: 12788
Utgivare: NATURE PUBLISHING GROUP

SLU författare

• Jonsson, Kristoffer

  • Institutionen för skoglig genetik och växtfysiologi, Sveriges lantbruksuniversitet
    

• Bhalerao, Rupali R.

  • Institutionen för skoglig genetik och växtfysiologi, Sveriges lantbruksuniversitet
    

UKÄ forskningsämne

Botanik


Publikationens identifierare

DOI: https://doi.org/10.1038/ncomms12788

Permanent länk till denna sida (URI)

https://res.slu.se/id/publ/80796