The Mechanochemistry of Endocytosis
Open accessAbstract
Endocytic vesicle formation is a complex process that couples sequential protein recruitment and lipid modifications with dramatic shape transformations of the plasma membrane. Although individual molecular players have been studied intensively, how they all fit into a coherent picture of endocytosis remains unclear. That is, how the proper temporal and spatial coordination of endocytic events is achieved and what drives vesicle scission are not known. Drawing upon detailed knowledge from experiments in yeast, we develop the first integrated mechanochemical model that quantitatively recapitulates the temporal and spatial progression of endocytic events leading to vesicle scission. The central idea is that membrane curvature is coupled to the accompanying biochemical reactions. This coupling ensures that the process is robust and culminates in an interfacial force that pinches off the vesicle. Calculated phase diagrams reproduce endocytic mutant phenotypes observed in experiments and predict unique testable endocytic phenotypes in yeast and mammalian cells. The combination of experiments and theory in this work suggest a unified mechanism for endocytic vesicle formation across eukaryotes.
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Endocytic proteins such as Synaptojanin 1, Endophilin A, Syndapin 1, and Dynamin 1 can further curve the membrane and generate vesicles.
“Thereafter, endocytic proteins such as Synaptojanin 1, Endophilin A, Syndapin 1, and Dynamin 1 can further curve the membrane and generate vesicles47–50.”
From Membrane compression by synaptic vesicle exocytosis triggers ultrafast endocytosis (2023) · cites this paper as [47]
The Introduction says BAR-domain proteins can deform membranes, and the Results link yeast synaptojanin’s PIP2 hydrolysis to vesicle scission. The Introduction also describes dynamin GTPases as proposed to constrict membrane tubules. Our copy does not establish the claimed membrane-curving and vesicle-generating roles for all four named proteins, particularly Syndapin 1; much of the model concerns yeast proteins rather than the specific proteins listed. (LLM, conf=0.85)
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Self-citation
- Authors
- Liu, J., Sun, Y., Drubin, D. G., & Oster, G. F.
- Affiliations
- University of California, Berkeley (US)
- Corresponding author
- Drubin, David G.
- Oster, George F.
- Venue
- PLoS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2009-09-29
- Volume
- 7
- Issue
- 9
- Pages
- e1000204
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- PMC
- PMC2742711
- OpenAlex
- W2019040974
- Cited by
- 222
- References
- 59
- Citations by year
- 2026: 1 · 2025: 7 · 2024: 8 · 2023: 6 · 2022: 9 · 2021: 11 · 2020: 6 · 2019: 9 · 2018: 15 · 2017: 15 · 2016: 10 · 2015: 16 · 2014: 21 · 2013: 17 · 2012: 24
- FWCI
- 10.53
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Biology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- National Science Foundation (0414039)
- National Institute of General Medical Sciences (1 R01 GM 50399, R01GM042759, R01GM050399, 1 R01 GM 42759)
- 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 › Molecular Biology › Fungal and yeast genetics research
- Keywords
- endocytosis, mechanochemistry, vesicle scission, membrane curvature, protein recruitment, lipid modification, interfacial forces, mechanochemical model, phase diagram, vesicle formation
- MeSH terms
- Actins, Animals, Biomechanical Phenomena, Cell Membrane, Endocytosis, Saccharomycetales, Hydrolysis, Lipids, Mammals, Models, Biological, Phosphoric Monoester Hydrolases, Time Factors, Protein Structure, Tertiary, Phosphatidylinositol 4,5-Diphosphate, Transport Vesicles, Feedback, Physiological, Saccharomyces cerevisiae Proteins
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