Identification of a vesicular nucleotide transporter
Open accessAbstract
ATP is a major chemical transmitter in purinergic signal transmission. Before secretion, ATP is stored in secretory vesicles found in purinergic cells. Although the presence of active transport mechanisms for ATP has been postulated for a long time, the proteins responsible for its vesicular accumulation remains unknown. The transporter encoded by the human and mouse SLC17A9 gene, a novel member of an anion transporter family, was predominantly expressed in the brain and adrenal gland. The mouse and bovine counterparts were associated with adrenal chromaffin granules. Proteoliposomes containing purified transporter actively took up ATP, ADP, and GTP by using membrane potential as the driving force. The uptake properties of the reconstituted transporter were similar to that of the ATP uptake by synaptic vesicles and chromaffin granules. Suppression of endogenous SLC17A9 expression in PC12 cells decreased exocytosis of ATP. These findings strongly suggest that SLC17A9 protein is a vesicular nucleotide transporter and should lead to the elucidation of the molecular mechanism of ATP secretion in purinergic signal transmission.
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Nucleotide uptake into insulin secretory vesicles is mediated by vNUT (Slc17a9/SLC17A9).
“Nucleotide uptake into insulin secretory vesicles is mediated by the vesicular nucleotide transporter (vNUT, encoded by Slc17a9/SLC17A9) (596), which is expressed in mouse β-cells(3, 146).”
From Pancreatic β-Cell Electrical Activity and Insulin Secretion: Of Mice and Men (2018) · cites this paper as [596]
The paper identifies SLC17A9 as VNUT and reports nucleotide uptake by the purified transporter (Identification of a vesicular nucleotide transporter; Results and Discussion, page numbers unavailable). It examines chromaffin granules and PC12-cell secretory granules, but does not establish that VNUT mediates uptake into insulin secretory vesicles. (LLM, conf=0.86)
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- Authors
- Sawada, K., Echigo, N., Juge, N., Miyaji, T., Otsuka, M., Omote, H., Yamamoto, A., & Moriyama, Y.
- Affiliations
- Okayama University (JP)
- Nagahama Institute of Bio-Science and Technology (JP)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2008-04-15
- Volume
- 105
- Issue
- 15
- Pages
- 5683-5686
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2311367
- OpenAlex
- W1964988229
- Cited by
- 418
- References
- 0
- Citations by year
- 2026: 12 · 2025: 13 · 2024: 15 · 2023: 12 · 2022: 18 · 2021: 21 · 2020: 21 · 2019: 31 · 2018: 21 · 2017: 25 · 2016: 31 · 2015: 27 · 2014: 27 · 2013: 31 · 2012: 37
- FWCI
- 14.18
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- Okayama University Scientific Achievement Repository (Okayama University) (submittedVersion)
- Funders
- Japan Society for the Promotion of Science
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Physiology › Adenosine and Purinergic Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- vesicular nucleotide transporter, SLC17A9, ATP release, purinergic signaling, secretory vesicles, chromaffin granules, ATP uptake, exocytosis, PC12 cells, synaptic vesicles
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphate, Animals, Exocytosis, Guanosine Triphosphate, Humans, Nucleotides, Transfection, PC12 Cells, Nucleotide Transport Proteins, Vesicular Transport Proteins, Mice, Rats
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