Triacylglycerols sequester monotopic membrane proteins to lipid droplets.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
07 08 2020
07 08 2020
Historique:
received:
08
11
2019
accepted:
08
07
2020
entrez:
10
8
2020
pubmed:
10
8
2020
medline:
22
9
2020
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 32769983
doi: 10.1038/s41467-020-17585-8
pii: 10.1038/s41467-020-17585-8
pmc: PMC7414839
doi:
Substances chimiques
Lipid Bilayers
0
Membrane Proteins
0
Triglycerides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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