Self-propelling vesicles define glycolysis as the minimal energy machinery for neuronal transport
Open accessAbstract
The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) facilitates fast axonal transport in neurons. However, given that GAPDH does not produce ATP, it is unclear whether glycolysis per se is sufficient to propel vesicles. Although many proteins regulating transport have been identified, the molecular composition of transported vesicles in neurons has yet to be fully elucidated. Here we selectively enrich motile vesicles and perform quantitative proteomic analysis. In addition to the expected molecular motors and vesicular proteins, we find an enrichment of all the glycolytic enzymes. Using biochemical approaches and super-resolution microscopy, we observe that most glycolytic enzymes are selectively associated with vesicles and facilitate transport of vesicles in neurons. Finally, we provide evidence that mouse brain vesicles produce ATP from ADP and glucose, and display movement in a reconstituted in vitro transport assay of native vesicles. We conclude that transport of vesicles along microtubules can be autonomous.
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Glycolytic enzymes may be localized at the plasma membrane and on synaptic vesicles where major ion pumping is performed by transport ATPases.
“There is also evidence that the glycolytic enzymes may be localized right where the neuron most requires acute resupply of ATP: at the plasma membrane and on the synaptic vesicles where major ion pumping is performed by transport ATPases (Ikemoto et al., 2003; Dhar-Chowdhury et al., 2007; Hinckelmann et al., 2016).”
From Fueling thought: Management of glycolysis and oxidative phosphorylation in neuronal metabolism (2018) · cites this paper as Hinckelmann et al., 2016
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- Authors
- Hinckelmann, M.-V., Virlogeux, A., Niehage, C., Poujol, C., Choquet, D., Hoflack, B., Zala, D., & Saudou, F.
- Affiliations
- Université Paris-Sud (FR)
- Biotechnologisches Zentrum (DE)
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Saudou, Frédéric
- ORCID
- Venue
- Nature Communications
- Published
- 2016-10-24
- Volume
- 7
- Issue
- 1
- Pages
- 13233-13233
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC5078996
- OpenAlex
- W2538630917
- Cited by
- 103
- References
- 46
- Citations by year
- 2026: 5 · 2025: 11 · 2024: 11 · 2023: 11 · 2022: 11 · 2021: 17 · 2020: 12 · 2019: 7 · 2018: 10 · 2017: 8
- FWCI
- 5.71
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Agence Nationale de la Recherche (ANR-14-CE35-0027, ANR-12, ANR-12-BLAN-SVSE2)
- Institut National de la Santé et de la Recherche Médicale
- Fondation Bettencourt Schueller
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- axonal transport, glycolysis, glyceraldehyde-3-phosphate dehydrogenase, vesicle motility, neuronal transport, microtubules, ATP production, glycolytic enzymes, vesicle proteome, brain vesicles
- MeSH terms
- Adenosine Triphosphate, Animals, Brain, Cells, Cultured, Energy Metabolism, Glyceraldehyde-3-Phosphate Dehydrogenases, Glycolysis, Mice, Transgenic, Microtubules, Neurons, Proteome, Transport Vesicles, Proteomics, Mice, Rats
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