The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow
Open accessPreprint — published as 10.1016/j.ceb.2024.102377 · Paper page
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 other 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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Research works printed but not linked: 90
- 2023, RBG motif bridge-like lipid transport proteins: structure, functions, and open questions, Annu. Rev. Cell. Dev. Biol, 39, 409, 10.1146/annurev-cellbio-120420-014634 · DOI
- 10.1083/jcb.201807019 · DOI
- 10.1083/jcb.201610032 · DOI
- 10.1038/s41580-018-0071-5 · DOI · Paper page
- 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. · DOI · Paper page
- 10.1016/J.TCB.2022.03.011 · DOI
- 2020, Cryo-EM reconstruction of a VPS13 fragment reveals a long groove to channel lipids between membranes, J. Cell Biol, 219, e202001161, 10.1083/jcb.202001161 · DOI
- 10.1083/jcb.201811139 · DOI
- 10.1083/jcb.201104062 · DOI
- 10.1126/science.aab1370 · DOI
- 2022, Quantitative models of lipid transfer and membrane contact formation, Contact, 5, 1
- 10.1073/pnas.2101562118 · DOI
- 2021, TMEM41B and VMP1 are scramblases and regulate the distribution of cholesterol and phosphatidylserine, J. Cell Biol, 220, e202103105, 10.1083/jcb.202103105 · DOI
- 10.1038/s41594-020-00518-w · DOI · Paper page
- 10.1073/PNAS.2205425119/SUPPL_FILE/PNAS.2205425119.SM02.MP4 · DOI
- 2022, TMEM16 scramblases thin the membrane to enable lipid scrambling, Nat Commun, 13, 2604, 10.1038/s41467-022-30300-z · DOI
- 2023, Regulation of phospholipid distribution in the lipid bilayer by flippases and scramblases, Nat. Rev. Mol. Cell Bio, 24, 576, 10.1038/s41580-023-00604-z · DOI
- 10.1016/j.molcel.2022.10.017 · DOI
- 10.1038/nature23649 · DOI
- 10.1073/pnas.2015556117 · DOI
- Cooper BF , Clark R , Kudhai A , Bhabha G , Ekiert DC , Khalid S , Isom GL : Phospholipid transport to the bacterial outer membrane through an envelope-spanning bridge. bioRxiv preprint: https://www.biorxiv.org/content/10.1101/2023.10.05.561070v1 2023. · DOI
- 10.1083/jcb.201410071 · DOI
- 10.1016/J.CELL.2018.09.054 · DOI · Paper page
- 2020, Do cell membranes flow like honey or jiggle like jello?, Bioessays, 42, e1900142, 10.1002/bies.201900142 · DOI
- 10.1038/17806 · DOI
- 10.1083/jcb.201603108 · DOI
- 10.1126/science.1232251 · DOI
- 10.1126/science.1191054 · DOI
- 10.1016/j.cub.2007.09.039 · DOI
- 10.1016/j.devcel.2009.04.003 · DOI
- Phillips R : Membranes by the numbers. In Physics of Biological Membranes. Edited by Bassereau P , Sens P : Springer Nature; 2018:73–105. · DOI
- 10.1016/j.cell.2023.05.014 · DOI
- 10.1146/annurev.biophys.34.040204.144637 · DOI
- 10.1016/j.cub.2020.02.053 · DOI
- Friedman JR : Mitochondria from the Outside in: The Relationship Between Inter-Organelle Crosstalk and Mitochondrial Internal Organization. Contact 2022, 5 · DOI
- Bragulat-Teixidor H , Ishihara K , Szucs GM , Otsuka S : The junctions connecting the endoplasmic reticulum to the nuclear envelope are constricted and remodelled during the cell cycle. BioRxiv Preprint: https://www.biorxiv.org/content/10.1101/2023.01.31.526419v1 2023, · DOI
- 10.1126/science.aaz7714 · DOI
- 10.1016/j.devcel.2015.06.007 · DOI
- 2022, Rapid propagation of membrane tension at retinal bipolar neuron presynaptic terminals, Science Advances, 8, eabl4411, 10.1126/sciadv.abl4411 · DOI · Paper page
- 10.1016/S0006-3495(99)77168-7 · DOI
- 10.1126/sciadv.abo1297 · DOI
- 2019, Osmosis, from molecular insights to large-scale applications, Chem Soc Rev, 48, 3102, 10.1039/C8CS00420J · DOI
- Phillips R , Kondev J , Theriot J , Garcia H : Physical Biology of the Cell edn 2nd: Garland Science; 2012. · DOI
- 2022, In situ structural analysis reveals membrane shape transitions during autophagosome formation, Proc. Natl. Acad. Sci. USA, 119, e2209823119, 10.1073/pnas.2209823119 · DOI
- 2022, The many faces of membrane tension: Challenges across systems and scales, Biochim Biophys Acta Biomembr, 1864, 183897, 10.1016/j.bbamem.2022.183897 · DOI
- Aronson PS , Boron WF , Boulpaep EL : Transport of Solutes and Water. In Medical Physiology, edn 3. Edited by: Elsevier; 2016:102–140.
- Lipowsky R : Understanding giant vesicles: A theoretical perspective. In The Giant Vesicle Book. Edited by Dimova R, Marques CM: CRC Press; 2019:96. · DOI
- 10.1016/j.chemphyslip.2014.05.001 · DOI
- 1995, The concept of effective tension for fluctuating vesicles, Z Phys B Con Mat, 97, 299, 10.1007/BF01307480 · DOI
- 1984, Lipid exchange between membranes, Biophys. J, 46, 687, 10.1016/S0006-3495(84)84067-9 · DOI
- 2022, Fluorescent indicators for imaging membrane potential of organelles, Curr. Opin. Chem. Biol, 71, 102203, 10.1016/j.cbpa.2022.102203 · DOI
- 2023, Identification of a drug binding pocket in TMEM16F calcium-activated ion channel and lipid scramblase, Nat Commun, 14, 4874, 10.1038/s41467-023-40410-x · DOI
- 10.1016/j.celrep.2019.06.023 · DOI
- 10.1038/ncomms7671 · DOI
- Melia TJ : Growing thin-How bulk lipid transport drives expansion of the autophagosome membrane but not of its lumen. Curr. Opin. Cell Biol. 2023, 83 · DOI
- 10.1146/annurev-fluid-071320-095958 · DOI
- 10.1073/pnas.1306447110 · DOI
- 10.1101/2023.1103.1122.533804 · DOI
- 2021, Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport, Bba-Mol Cell Biol L, 1866, 159003
- 10.1091/mbc.E07-12-1292 · DOI · Paper page
- 2020, Inducible intracellular membranes: molecular aspects and emerging applications, Microb Cell Fact, 19, 176, 10.1186/s12934-020-01433-x · DOI
- 10.1083/jcb.107.1.101 · DOI
- 10.1073/pnas.0903353106 · DOI
- 2020, Modeling membrane morphological change during autophagosome formation, Iscience, 23, 101466, 10.1016/j.isci.2020.101466 · DOI
- 10.1083/JCB.202002085 · DOI
- 10.7554/eLife.45777 · DOI
- 2019, Atg2 mediates direct lipid transfer between membranes for autophagosome formation, Nat. Struct. Mol. Biol, 26, 281, 10.1038/s41594-019-0203-4 · DOI
- 2020, Engineering lipid membranes with programmable DNA nanostructures, Adv Biosyst, 4, 1900215, 10.1002/adbi.201900215 · DOI
- 10.1016/j.bpj.2021.11.2884 · DOI
- 2022, Stepwise membrane binding of extended synaptotagmins revealed by optical tweezers, Nat. Chem. Biol, 18, 313, 10.1038/s41589-021-00914-3 · DOI
- 10.7554/eLife.30493 · DOI
- 2022, Suspended lipid bilayer: a versatile platform for nextgen drug discovery and biomedical applications, Accounts Mater Res, 3, 996, 10.1021/accountsmr.2c00157 · DOI
- 10.1038/s41557-018-0127-3 · DOI
- 10.1103/PhysRevLett.88.238101 · DOI
- 10.1038/nchem.2472 · DOI
- 2021, Sorting sub-150-nm liposomes of distinct sizes by DNA-brick-assisted centrifugation, Nat Chem, 13, 335, 10.1038/s41557-021-00667-5 · DOI
- 10.1039/C2FD20108A · DOI
- 10.1038/s41589-019-0325-3 · DOI
- 2023, Functionalization and higher-order organization of liposomes with DNA nanostructures, Nat Commun, 14, 5256, 10.1038/s41467-023-41013-2 · DOI
- 2021, Reconstitution of contractile actomyosin rings in vesicles, Nat Commun, 12, 2254, 10.1038/s41467-021-22422-7 · DOI
- 10.1038/s41567-019-0464-1 · DOI
- 2023, Engineering DNA-based cytoskeletons for synthetic cells, Interface Focus, 13, 20230028, 10.1098/rsfs.2023.0028 · DOI
- 2018, Vesicle tubulation with self-assembling DNA nanosprings, Angew Chem Int Edit, 57, 5330, 10.1002/anie.201800141 · DOI
- 2021, Reversible membrane deformations by straight DNA origami filaments, Soft Matter, 17, 276, 10.1039/D0SM00150C · DOI
- 10.1038/s41467-018-03198-9 · DOI
- 2021, Proton gradients from light-harvesting control DNA assemblies for synthetic cells, Nat Commun, 12, 3967, 10.1038/s41467-021-24103-x · DOI
- 2022, Bottom-up assembly of synthetic cells with a DNA cytoskeleton, Acs Nano, 16, 7233, 10.1021/acsnano.1c10703 · DOI
- 2022, Actuating tension-loaded DNA clamps drives membrane tubulation, Science Advances, 8, eadd1830, 10.1126/sciadv.add1830 · DOI
- 2023, A membrane tension-responsive mechanosensitive DNA nanomachine, Angew Chem Int Edit, 62, e20230589
- 2018, A synthetic enzyme built from DNA flips 107 lipids per second in biological membranes, Nat Commun, 9, 2426, 10.1038/s41467-018-04821-5 · DOI
Metadata
- Authors
- Zhang, Y., & Lin, C.
- Affiliations
- Yale University (US)
- Corresponding author
- Zhang, Yongli
- Lin, Chenxiang
- Venue
- Current Opinion in Cell Biology
- Publisher
- openRxiv
- Published
- 2024-01-08
- Volume
- 88
- Pages
- 102377-102377
- ISSN
- 0955-0674 (ISSN-L)
- PMC
- PMC11193448
- OpenAlex
- W4399239987
- Cited by
- 14
- References
- 1
- Citations by year
- 2026: 7 · 2025: 6 · 2024: 1
- FWCI
- 0.57
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Current Opinion in Cell Biology (acceptedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- PubMed Central (submittedVersion, cc-by-nc-nd)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R35GM131714, R35GM149264)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- membrane tension, lipid flow, lipid transfer proteins, scramblase, lipid homeostasis, organelle biogenesis, membrane domains
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow. https://app.cochat.ai/papers/10.1101/2024.01.08.574656
- The paper
- Zhang, Y., & Lin, C. (2024). Lipid osmosis, membrane tension, and other mechanochemical driving forces of lipid flow. Current Opinion in Cell Biology. https://doi.org/10.1101/2024.01.08.574656