ArticleThe Journal of biological chemistry2016
A Plasma Membrane Association Module in Yeast Amino Acid Transporters.
Article in The Journal of biological chemistry, 2016. 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, 22 citations in OpenAlex.
- Glucose repression ofbioRxiv : the preprint server for biology · 2026Article
- Systematic Engineering for Efficient Uric Acid-Degrading Activity in Probiotic YeastACS synthetic biology · 2025Article
- Article
- Palmitoylation at a conserved cysteine residue facilitates gasdermin D-mediated pyroptosis and cytokine release.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Extracellular loops matter - subcellular location and function of the lysine transporter Lyp1 from Saccharomyces cerevisiae.The FEBS journal · 2020Article
- A Trifunctional Linker for Palmitoylation and Peptide and Protein Localization in Biological Membranes.Chembiochem : a European journal of chemical biology · 2020Article
- Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019Review
- Tales of tails in transporters.Open biology · 2019Review
- Arabidopsis UMAMIT24 and 25 are amino acid exporters involved in seed loading.Journal of experimental botany · 2018Article
- Amino Acid Metabolism and Transport Mechanisms as Potential Antifungal Targets.International journal of molecular sciences · 2018Review
- Steric exclusion and protein conformation determine the localization of plasma membrane transporters.Nature communications · 2018Article
Corrections and comments
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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
Amino acid permeases (AAPs) in the plasma membrane (PM) of Saccharomyces cerevisiae are responsible for the uptake of amino acids and involved in regulation of their cellular levels. Here, we report on a strong and complex module for PM association found in the C-terminal tail of AAPs. Using in silico analyses and mutational studies we found that the C-terminal sequences of Gap1, Bap2, Hip1, Tat1, Tat2, Mmp1, Sam3, Agp1, and Gnp1 are about 50 residues long, associate with the PM, and have features that discriminate them from the termini of organellar amino acid transporters. We show that this sequence (named PMasseq) contains an amphipathic α-helix and the FWC signature, which is palmitoylated by palmitoyltransferase Pfa4. Variations of PMasseq, found in different AAPs, lead to different mobilities and localization patterns, whereas the disruption of the sequence has an adverse effect on cell viability. We propose that PMasseq modulates the function and localization of AAPs along the PM. PMasseq is one of the most complex protein signals for plasma membrane association across species and can be used as a delivery vehicle for the PM.
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