Membrane Hemifusion: Crossing a Chasm in Two Leaps
Open accessAbstract
During membrane fusion, the outer leaflets of the two membranes merge first, whereas the distal membrane leaflets remain separate until the opening of a fusion pore. This intermediate stage, called hemifusion, is a critical event shared by exocytosis, protein trafficking, and viral entry.
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Lipid headgroups forming membrane surfaces are highly hydrophilic and hydrated, imposing a high energy barrier for two membranes to fuse due to hydration repulsion.
“The lipidic headgroups forming the membranes' surface are highly hydrophilic and hydrated, imposing a high energy barrier for two membranes to fuse due to hydration repulsion [4][5][6][7] .”
From Fusion of lipid membranes: an alternative pathway (2026) · cites this paper as [4]
The passage on close membrane apposition (labelled Abstract in our copy; no page given) says that intermembrane hydration repulsion builds as membrane spacing decreases and that a forming stalk can release this hydration energy. It does not explicitly say that the lipid headgroups are highly hydrophilic and hydrated, and it describes hydration repulsion’s role in hemifusion as likely rather than stating the full causal explanation as fact. (LLM, conf=0.82)
Experimental — accuracy not yet measuredElectropores promote metastable interbilayer splays, lowering the energy barrier for peripore stalk formation even at membrane separations >1 nm, conditions under which strong hydration repulsion would otherwise hinder stalk formation.
“Our proposed membrane fusion pathway centers on electropores, which promote metastable interbilayer splays, lowering the energy barrier for peripore stalk formation even at membrane separations >1 nm -conditions under which strong hydration repulsion would otherwise hinder stalk formation 4,7,37 .”
From Fusion of lipid membranes: an alternative pathway (2026) · cites this paper as [4]
The passage labeled Abstract (page unavailable) discusses stalk formation, lipid-tail splaying, and the balance between stalk elastic energy and hydration repulsion at close membrane spacing. It does not say that electropores create metastable interbilayer splays or lower the barrier for peripore stalk formation at separations greater than 1 nm. (LLM, conf=0.85)
Experimental — accuracy not yet measuredFusogenic proteins mediate membrane fusion by pulling the membranes into contact to overcome the high energy barrier imposed by hydration repulsion.
“It is often considered in the presence of fusogenic proteins, which mediate the fusion by pulling the membranes into contact to overcome the high energy barrier imposed by hydration repulsion [4][5][6][7] .”
From Fusion of lipid membranes: an alternative pathway (2026) · cites this paper as [4]
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Research works printed but not linked: 5
- [1]1. Armstrong, R.T. ∙ Kushnir, A.S. ∙ White, J.M. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition J. Cell Biol. 2000; 151:425-438 Crossref Scopus (180) PubMed Google Scholar
- [2]2. Blumenthal, R. ∙ Clague, M.J. ∙ Durell, S.R. ... Membrane fusion Chem. Rev. 2003; 103:53-69 Crossref Scopus (246) PubMed Google Scholar
- [3]3. Chernomordik, L.V. ∙ Kozlov, M.M. Protein-lipid interplay in fusion and fission of biological membranes Annu. Rev. Biochem. 2003; 72:175-207 Crossref Scopus (633) PubMed Google Scholar
- [4]4. Chernomordik, L.V. ∙ Melikyan, G.B. ∙ Chizmadzhev, Y.A. Biomembrane fusion: a new concept derived from model studies using two interacting planar lipid bilayers Biochim. Biophys. Acta. 1987; 906:309-352 Crossref Scopus (278) PubMed Google Scholar
- [5]5. Chernomordik, L.V. ∙ Vogel, S.S. ∙ Sokoloff, A. ... Lysolipids reversibly inhibit Ca(2+)-, GTP- and pH-dependent fusion of biological membranes FEBS Lett. 1993; 318:71-76
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Distribution and Apoptotic Function of Outer Membrane Proteins Depend on Mitochondrial Fusion
Weaver, D., Eisner, V., Liu, X., Várnai, P., Hunyady, L., Gross, A., & Hajnóczky, G. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.048 · Cited by 58 · see citing works
Fusion of lipid membranes: an alternative pathway
Jin, D., Li, Z., Roke, S., & Klein, J. (2026) · doi:10.64898/2026.02.19.706911
- Authors
- Chernomordik, L. V., & Kozlov, M. M.
- Affiliations
- National Institutes of Health (US)
- Tel Aviv University (IL)
- Corresponding author
- Chernomordik, Leonid V.
- Kozlov, Michael M.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2005-11
- Volume
- 123
- Issue
- 3
- Pages
- 375-382
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2170902894
- Cited by
- 376
- References
- 0
- Citations by year
- 2026: 12 · 2025: 5 · 2024: 13 · 2023: 14 · 2022: 15 · 2021: 18 · 2020: 7 · 2019: 15 · 2018: 6 · 2017: 18 · 2016: 13 · 2015: 19 · 2014: 27 · 2013: 14 · 2012: 32
- FWCI
- 2.17
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Keywords
- membrane fusion, fusion pore, exocytosis, protein trafficking, viral entry, lipid bilayers
- MeSH terms
- Animals, Cell Membrane, Exocytosis, Humans, Lipid Bilayers, Membrane Fusion, Virus Physiological Phenomena, Protein Transport, SNARE Proteins
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