ArticleCell research2018
Succinate-acetate permease from Citrobacter koseri is an anion channel that unidirectionally translocates acetate.
Article in Cell research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 13 citations in OpenAlex.
- Functional In Vitro Expression of the Succinate-Acetate Transporter SatP and an Initial Screening Strategy.Membranes · 2026Article
- Expansion, functional diversification, and gene fusion events in the Ato protein family.iScience · 2026Article
- ThemBio · 2025Article
- The Dicarboxylate Transporters from the AceTr Family and Dct-02 Oppositely Affect Succinic Acid Production inJournal of fungi (Basel, Switzerland) · 2022Article
- Uncovering Novel Plasma Membrane Carboxylate Transporters in the YeastJournal of fungi (Basel, Switzerland) · 2022Article
- Solid-State NMR Studies of the Succinate-Acetate Permease from Citrobacter Koseri in Liposomes and Native Nanodiscs.Life (Basel, Switzerland) · 2021Article
- New insights into the acetate uptake transporter (AceTr) family: Unveiling amino acid residues critical for specificity and activity.Computational and structural biotechnology journal · 2021Article
- Carboxylic Acid Transporters inmBio · 2020Review
- TScientific reports · 2019Article
- Article
- Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements.Journal of biomolecular NMR · 2019Article
- Crystal structure of the bacterial acetate transporter SatP reveals that it forms a hexameric channel.The Journal of biological chemistry · 2018Article
- The physiological effect of heavy metals and volatile fatty acids onBiotechnology for biofuels · 2018Article
Corrections and comments
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Authors and funding
14 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acetate is an important metabolite in metabolism and cell signaling. Succinate-Acetate Permease (SatP) superfamily proteins are known to be responsible for acetate transport across membranes, but the nature of this transport remains unknown. Here, we show that the SatP homolog from Citrobacter koseri (SatP_Ck) is an anion channel that can unidirectionally translocate acetate at rates of the order of ~10
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