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Review
. 2024 Jun:88:102377.
doi: 10.1016/j.ceb.2024.102377. Epub 2024 May 31.

Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow

Affiliations
Review

Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow

Yongli Zhang et al. Curr Opin Cell Biol. 2024 Jun.

Abstract

Nonvesicular lipid transport among different membranes or membrane domains plays crucial roles in lipid homeostasis and organelle biogenesis. However, the forces that drive such lipid transport are not well understood. We propose that lipids tend to flow towards the membrane area with a higher membrane protein density in a process termed lipid osmosis. This process lowers the membrane tension in the area, resulting in a membrane tension difference called osmotic membrane tension. We examine the thermodynamic basis and experimental evidence of lipid osmosis and osmotic membrane tension. We predict that lipid osmosis can drive bulk lipid flows between different membrane regions through lipid transfer proteins, scramblases, or similar barriers that selectively pass lipids but not membrane proteins. We also speculate on the biological functions of lipid osmosis. Finally, we explore other driving forces for lipid transfer and describe potential methods and systems to further test our theory.

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Conflict of interest statement

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

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References

    1. Hanna M, Guillen-Samander A, De Camilli P: RBG motif bridge-like lipid transport proteins: structure, functions, and open questions. Annu. Rev. Cell. Dev. Biol 2023, 39:409–434 - PubMed
    1. Kumar N, Leonzino M, Hancock-Cerutti W, Horenkamp FA, Li P, Lees JA, Wheeler H, Reinisch KM, De Camilli P: VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites. J. Cell Biol 2018, 217:3625–3639 - PMC - PubMed
    1. Reinisch KM, Prinz WA: Mechanisms of nonvesicular lipid transport. J. Cell Biol 2021, 220:e202012058 - PMC - PubMed
    1. Wong LH, Gatta AT, Levine TP: Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes. Nat. Rev. Mol. Cell Bio 2019, 20:85–101 - PubMed
    1. Cai SJ, Wu YM, Guillen-Samander A, Hancock-Cerutti W, Liu J, De Camilli P: In situ architecture of the lipid transport protein VPS13C at ER-lysosome membrane contacts. Proc. Natl. Acad. Sci. USA 2022, 119. - PMC - PubMed
    2. **Using Cryo-EM and AlphaFold structural predictions, the authors develop an in situ architecture of VPS13C at the membrane contact site between ER and lysosome. The membrane spacing at the contact site decreases when VPS13C is truncated to a shorter version, indicating a role of VPS13C in bridging the two membranes. Overall, the structural characterization corroborates VPS13C as a bridge LTP.

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