ArticleThe Biochemical journal2005
Kinetics of bidirectional H+ and substrate transport by the proton-dependent amino acid symporter PAT1.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 32 citations in OpenAlex.
- Exploring Amino Acid Transporters as Therapeutic Targets for Cancer: An Examination of Inhibitor Structures, Selectivity Issues, and Discovery Approaches.Pharmaceutics · 2024Review
- The Concise Guide to PHARMACOLOGY 2013/14: transporters.British journal of pharmacology · 2013Article
- Function and expression of the proton-coupled amino acid transporter PAT1 along the rat gastrointestinal tract: implications for intestinal absorption of gaboxadol.British journal of pharmacology · 2012Article
- An integrated field-effect microdevice for monitoring membrane transport in Xenopus laevis oocytes via lateral proton diffusion.PloS one · 2012Article
- The SLC36 family of proton-coupled amino acid transporters and their potential role in drug transport.British journal of pharmacology · 2011Review
- The proton-coupled amino acid transporter, SLC36A1 (hPAT1), transports Gly-Gly, Gly-Sar and other Gly-Gly mimetics.British journal of pharmacology · 2010Article
- Effects of Na+ and H+ on steady-state and presteady-state currents of the human concentrative nucleoside transporter 3 (hCNT3).Pflugers Archiv : European journal of physiology · 2010Article
- Characterization of a blood-meal-responsive proton-dependent amino acid transporter in the disease vector, Aedes aegypti.The Journal of experimental biology · 2009Article
- Identification of a disulfide bridge essential for transport function of the human proton-coupled amino acid transporter hPAT1.The Journal of biological chemistry · 2009Article
- Role of the glutamate 185 residue in proton translocation mediated by the proton-coupled folate transporter SLC46A1.American journal of physiology. Cell physiology · 2009Article
- The functional roles of the His247 and His281 residues in folate and proton translocation mediated by the human proton-coupled folate transporter SLC46A1.The Journal of biological chemistry · 2009Article
- The molecular basis of neutral aminoacidurias.Pflugers Archiv : European journal of physiology · 2006Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PAT1 is a recently identified member of the PAT family of proton/amino acid co-transporters with predominant expression in the plasma membrane of enterocytes and in lysosomal membranes of neurons. Previous studies in Xenopus oocytes expressing PAT1 established proton/substrate co-transport associated with positive inward currents for a variety of small neutral amino acids. Here we provide a detailed analysis of the transport mode of the murine PAT1 in oocytes using the two-electrode voltage-clamp technique to measure steady-state and pre-steady-state currents. The GPC (giant patch clamp) technique and efflux studies were employed to characterize the reversed transport mode. Kinetic parameters [K(m) (Michaelis constant) and I(max) (maximum current)] for transport of various substrates revealed a dependence on membrane potential: hyperpolarization increases the substrate affinity and maximal transport velocity. Proton affinity for interaction with PAT1 is almost 100 nM, corresponding to a pH of 7.0 and is independent of substrate. Kinetic analysis revealed that binding of proton most likely occurs before substrate binding and that the proton and substrate are translocated in a simultaneous step. No evidence for a substrate-uncoupled proton shunt was observed. As shown by efflux studies and current measurements by the GPC technique, PAT1 allows bidirectional amino acid transport. Surprisingly, PAT1 exhibits no pre-steady-state currents in the absence of substrate, even at low temperatures, and therefore PAT1 takes an exceptional position among the ion-coupled co-transporters.
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