PUBLICATION

A conserved megaprotein-based molecular bridge critical for lipid trafficking and cold resilience

Authors
Wang, C., Wang, B., Pandey, T., Long, Y., Zhang, J., Oh, F., Sima, J., Guo, R., Liu, Y., Zhang, C., Mukherjee, S., Bassik, M., Lin, W., Deng, H., Vale, G., McDonald, J.G., Shen, K., Ma, D.K.
ID
ZDB-PUB-221115-68
Date
2022
Source
Nature communications   13: 6805 (Journal)
Registered Authors
Long, Yong
Keywords
none
MeSH Terms
  • Animals
  • Caenorhabditis elegans*/genetics
  • Caenorhabditis elegans*/metabolism
  • Cell Membrane/metabolism
  • Endoplasmic Reticulum/metabolism
  • Humans
  • Mammals/metabolism
  • Phospholipids/metabolism
  • Zebrafish*/genetics
  • Zebrafish*/metabolism
PubMed
36357390 Full text @ Nat. Commun.
Abstract
Cells adapt to cold by increasing levels of unsaturated phospholipids and membrane fluidity through conserved homeostatic mechanisms. Here we report an exceptionally large and evolutionarily conserved protein LPD-3 in C. elegans that mediates lipid trafficking to confer cold resilience. We identify lpd-3 mutants in a mutagenesis screen for genetic suppressors of the lipid desaturase FAT-7. LPD-3 bridges the endoplasmic reticulum (ER) and plasma membranes (PM), forming a structurally predicted hydrophobic tunnel for lipid trafficking. lpd-3 mutants exhibit abnormal phospholipid distribution, diminished FAT-7 abundance, organismic vulnerability to cold, and are rescued by Lecithin comprising unsaturated phospholipids. Deficient lpd-3 homologues in Zebrafish and mammalian cells cause defects similar to those observed in C. elegans. As mutations in BLTP1, the human orthologue of lpd-3, cause Alkuraya-Kucinskas syndrome, LPD-3 family proteins may serve as evolutionarily conserved highway bridges critical for ER-associated non-vesicular lipid trafficking and resilience to cold stress in eukaryotic cells.
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