ArticleCellular and molecular life sciences : CMLS2011
Functional and structural determinants of reverse operation in the pH-dependent oligopeptide transporter PepT1.
Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 12 citations in OpenAlex.
- Functional characterization of Atlantic salmon (Salmo salar L.) PepT2 transporters.The Journal of physiology · 2022Article
- Di- and tripeptide transport in vertebrates: the contribution of teleost fish models.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017Review
- Amino acid transporter B(0)AT1 (slc6a19) and ancillary protein: impact on function.Pflugers Archiv : European journal of physiology · 2016Article
- Temperature effects on the kinetic properties of the rabbit intestinal oligopeptide cotransporter PepT1.Pflugers Archiv : European journal of physiology · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The functional and structural basis of reverse operation of PepT1 has been studied in Xenopus oocytes expressing the wild-type and mutated forms of this protein. Using brief pulses from a negative holding potential, wild-type and Arg282 mutants exhibit outward currents in the presence of Gly-Gln. The reversal potential of these currents is affected by both pH and substrate concentration, confirming coupled transport in the wild type and in the mutants as well. Long-lasting voltage and current-clamp experiments show that the outward currents are only temporary, and reflect accumulation and/or depletion effects near the membrane. The ability to operate in reverse mode was confirmed in all isoforms by intracellular injection of substrate. The role of Arg282 and Asp341 in the reverse transport was also investigated using charged substrates. Positive Lys-Gly (but not Gly-Lys) showed enhanced transport currents in the Arg282 mutants. In contrast, negative Gly-Asp and Asp-Gly elicited modest currents in all isoforms.
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