ArticleeLife2014
Thermodynamic evidence for a dual transport mechanism in a POT peptide transporter.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 69 citations in OpenAlex.
- Structural basis for transport and inhibition of nucleotide sugar transport in pathogenic fungi.Nature communications · 2026Article
- Fluorescence-Based Ion Transport Assays Using Proteoliposomes.Bio-protocol · 2026Article
- Structural basis of glucosinolate recognition and transport by plant GTR1.Cell discovery · 2026Article
- Structural basis for pH-responsive amino acid transport via SLC7A4.Nature communications · 2026Article
- Defined roles for the Staphylococcus aureus POT transporter DtpT in di/tripeptide uptake and glutathione utilisation inside human macrophages.PLoS pathogens · 2025Article
- Cryo-EM structures reveal the HLife science alliance · 2025Article
- Article
- MFSD1 with its accessory subunit GLMP functions as a general dipeptide uniporter in lysosomes.Nature cell biology · 2024Article
- Review
- Obstacles, research progress, and prospects of oral delivery of bioactive peptides: a comprehensive review.Frontiers in nutrition · 2024Review
- Structural basis for proton coupled cystine transport by cystinosin.Nature communications · 2022Article
- Experimental platform for the functional investigation of membrane proteins in giant unilamellar vesicles.Soft matter · 2022Article
- Assembly and Functional Role of PACE Transporter PA2880 from Pseudomonas aeruginosa.Microbiology spectrum · 2022Article
- General principles of secondary active transporter function.Biophysics reviews · 2022Review
- A solid-supported membrane electrophysiology assay for efficient characterization of ion-coupled transport.The Journal of biological chemistry · 2021Article
- Engineering and functional characterization of a proton-driven β-lactam antibiotic translocation module for bionanotechnological applications.Scientific reports · 2021Article
- Cryo-EM structure of PepT2 reveals structural basis for proton-coupled peptide and prodrug transport in mammals.Science advances · 2021Article
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- Membrane Chemistry Tunes the Structure of a Peptide Transporter.Angewandte Chemie (International ed. in English) · 2020Article
- Antidiabetic Food-Derived Peptides for Functional Feeding: Production, Functionality and In Vivo Evidences.Foods (Basel, Switzerland) · 2020Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Peptide transport plays an important role in cellular homeostasis as a key route for nitrogen acquisition in mammalian cells. PepT1 and PepT2, the mammalian proton coupled peptide transporters (POTs), function to assimilate and retain diet-derived peptides and play important roles in drug pharmacokinetics. A key characteristic of the POT family is the mechanism of peptide selectivity, with members able to recognise and transport >8000 different peptides. In this study, we present thermodynamic evidence that in the bacterial POT family transporter PepTSt, from Streptococcus thermophilus, at least two alternative transport mechanisms operate to move peptides into the cell. Whilst tri-peptides are transported with a proton:peptide stoichiometry of 3:1, di-peptides are co-transported with either 4 or 5 protons. This is the first thermodynamic study of proton:peptide stoichiometry in the POT family and reveals that secondary active transporters can evolve different coupling mechanisms to accommodate and transport chemically and physically diverse ligands across the membrane.
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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.