ArticleThe Journal of biological chemistry2014
Converting the yeast arginine can1 permease to a lysine permease.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 56 citations in OpenAlex.
- The Saccharomyces cerevisiae amino acid transporter Lyp1 has a broad substrate spectrum.FEBS letters · 2025Article
- Regulation of Arginine Metabolism and Ethanol Tolerance inFood science & nutrition · 2025Article
- Fitness landscape of substrate-adaptive mutations in evolved amino acid-polyamine-organocation transporters.eLife · 2024Article
- Screening ofFrontiers in microbiology · 2023Article
- A plant plasma-membrane HScientific reports · 2021Article
- Growth Inhibition by Amino Acids inMicroorganisms · 2020Article
- Extracellular loops matter - subcellular location and function of the lysine transporter Lyp1 from Saccharomyces cerevisiae.The FEBS journal · 2020Article
- Uptake of exogenous serine is important to maintain sphingolipid homeostasis in Saccharomyces cerevisiae.PLoS genetics · 2020Article
- Nitrogen coordinated import and export of arginine across the yeast vacuolar membrane.PLoS genetics · 2020Article
- Periprotein lipidomes ofeLife · 2020Article
- Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019Review
- In silico characterization of residues essential for substrate binding of human cystine transporter, xCT.Journal of molecular modeling · 2019Article
- Function and Regulation of Acid Resistance Antiporters.The Journal of membrane biology · 2019Article
- Tales of tails in transporters.Open biology · 2019Review
- Resistance to Two Vinylglycine Antibiotic Analogs Is Conferred by Inactivation of Two Separate Amino Acid Transporters inJournal of bacteriology · 2019Article
- Integration Through Separation - The Role of Lateral Membrane Segregation in Nutrient Uptake.Frontiers in cell and developmental biology · 2019Review
- Lateral plasma membrane compartmentalization links protein function and turnover.The EMBO journal · 2018Article
- On the Evolution of Specificity in Members of the Yeast Amino Acid Transporter Family as Parts of Specific Metabolic Pathways.International journal of molecular sciences · 2018Review
- Conformation-dependent partitioning of yeast nutrient transporters into starvation-protective membrane domains.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The yeast HeLife · 2018Article
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6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amino acid uptake in yeast cells is mediated by about 16 plasma membrane permeases, most of which belong to the amino acid-polyamine-organocation (APC) transporter family. These proteins display various substrate specificity ranges. For instance, the general amino acid permease Gap1 transports all amino acids, whereas Can1 and Lyp1 catalyze specific uptake of arginine and lysine, respectively. Although Can1 and Lyp1 have different narrow substrate specificities, they are close homologs. Here we investigated the molecular rules determining the substrate specificity of the H(+)-driven arginine-specific permease Can1. Using a Can1-Lyp1 sequence alignment as a guideline and a three-dimensional Can1 structural model based on the crystal structure of the bacterial APC family arginine/agmatine antiporter, we introduced amino acid substitutions liable to alter Can1 substrate specificity. We show that the single substitution T456S results in a Can1 variant transporting lysine in addition to arginine and that the combined substitutions T456S and S176N convert Can1 to a Lyp1-like permease. Replacement of a highly conserved glutamate in the Can1 binding site leads to variants (E184Q and E184A) incapable of any amino acid transport, pointing to a potential role for this glutamate in H(+) coupling. Measurements of the kinetic parameters of arginine and lysine uptake by the wild-type and mutant Can1 permeases, together with docking calculations for each amino acid in their binding site, suggest a model in which residues at positions 176 and 456 confer substrate selectivity at the ligand-binding stage and/or in the course of conformational changes required for transport.
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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.