ArticleThe Biochemical journal2016
The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding site.
Article in The Biochemical journal, 2016. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Enhancing prestin oligomerization for superior sonogenetics.Theranostics · 2026Article
- Sonogenetics for precision medicine: from molecular toolkit to clinical translation.Theranostics · 2026Review
- Asymmetric pendrin homodimer reveals its molecular mechanism as anion exchanger.Nature communications · 2023Article
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- Functional Parameters of Prestin Are Not Correlated With the Best Hearing Frequency.Frontiers in cell and developmental biology · 2021Article
- STAS Domain Only Proteins in Bacterial Gene Regulation.Frontiers in cellular and infection microbiology · 2021Review
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- Article
- Deletion of exons 17 and 18 in prestin's STAS domain results in loss of function.Scientific reports · 2019Article
- The E. coli dicarboxylic acid transporters DauA act as a signal transducer by interacting with the DctA uptake system.Scientific reports · 2017Article
- Chansporter complexes in cell signaling.FEBS letters · 2017Review
- Prestin and the good vibrations.The Biochemical journal · 2016Article
- The chloride-channel blocker 9-anthracenecarboxylic acid reduces the nonlinear capacitance of prestin-associated charge movement.The European journal of neuroscience · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prestin is a unique ATP- and Ca(2+)-independent molecular motor with piezoelectric characteristics responsible for the electromotile properties of mammalian cochlear outer hair cells, i.e. the capacity of these cells to modify their length in response to electric stimuli. This 'electromotility' is at the basis of the exceptional sensitivity and frequency selectivity distinctive of mammals. Prestin belongs to the SLC26 (solute carrier 26) family of anion transporters and needs anions to function properly, particularly Cl(-). In the present study, using X-ray crystallography we reveal that the STAS (sulfate transporter and anti-sigma factor antagonist) domain of mammalian prestin, considered an 'incomplete' transporter, harbours an unanticipated anion-binding site. In parallel, we present the first crystal structure of a prestin STAS domain from a non-mammalian vertebrate prestin (chicken) that behaves as a 'full' transporter. Notably, in chicken STAS, the anion-binding site is lacking because of a local structural rearrangement, indicating that the presence of the STAS anion-binding site is exclusive to mammalian prestin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.