期刊
ELIFE
卷 10, 期 -, 页码 -出版社
eLIFE SCIENCES PUBL LTD
DOI: 10.7554/eLife.61401
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资金
- Centre National de la Recherche Scientifique CNRS-PICS [214454]
- Slovenian Research Agency [P1-0055]
- Ministere de l'Enseignement Superieur et de la Recherche Scientifique
- Fondation ARC pour la Recherche sur le Cancer [DOC20190509052]
- European Research Council Synergy [856404]
- European Research Council (ERC) [856404] Funding Source: European Research Council (ERC)
This study reveals the mechanism by which Plin4 forms a stable protein layer on the surface of LDs, with the stability of its AHs on LDs being sensitive to the nature and distribution of its polar residues, suggesting a general mechanism of AH stabilization via lateral interactions.
Numerous proteins target lipid droplets (LDs) through amphipathic helices (AHs). It is generally assumed that AHs insert bulky hydrophobic residues in packing defects at the LD surface. However, this model does not explain the targeting of perilipins, the most abundant and specific amphipathic proteins of LDs, which are weakly hydrophobic. A striking example is Plin4, whose gigantic and repetitive AH lacks bulky hydrophobic residues. Using a range of complementary approaches, we show that Plin4 forms a remarkably immobile and stable protein layer at the surface of cellular or in vitro generated oil droplets, and decreases LD size. Plin4 AH stability on LDs is exquisitely sensitive to the nature and distribution of its polar residues. These results suggest that Plin4 forms stable arrangements of adjacent AHs via polar/electrostatic interactions, reminiscent of the organization of apolipoproteins in lipoprotein particles, thus pointing to a general mechanism of AH stabilization via lateral interactions.
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