Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow
- PMID: 38823338
- PMCID: PMC11193448
- DOI: 10.1016/j.ceb.2024.102377
Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow
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.
Copyright © 2024 Elsevier Ltd. All rights reserved.
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.
Update of
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Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow.bioRxiv [Preprint]. 2024 Apr 28:2024.01.08.574656. doi: 10.1101/2024.01.08.574656. bioRxiv. 2024. Update in: Curr Opin Cell Biol. 2024 Jun;88:102377. doi: 10.1016/j.ceb.2024.102377. PMID: 38260424 Free PMC article. Updated. Preprint.
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References
-
- 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
-
- 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
-
- 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
-
**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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