ArticleThe Journal of biological chemistry2015
Transport rates of a glutamate transporter homologue are influenced by the lipid bilayer.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 36 citations in OpenAlex.
- Membrane vectorial lipidomic features of coral host cells' plasma membrane and lipid profiles of their endosymbionts Cladocopium.Communications biology · 2024Article
- How physical forces drive the process of helical membrane protein folding.EMBO reports · 2022Review
- Elucidating the Mechanism Behind Sodium-Coupled Neurotransmitter Transporters by Reconstitution.Neurochemical research · 2022Review
- Reconstitution of GABA, Glycine and Glutamate Transporters.Neurochemical research · 2022Review
- Eugene P. Kennedy's Legacy: Defining Bacterial Phospholipid Pathways and Function.Frontiers in molecular biosciences · 2021Review
- Impact of nanodisc lipid composition on cell-free expression of proton-coupled folate transporter.PloS one · 2021Article
- How bilayer properties influence membrane protein folding.Protein science : a publication of the Protein Society · 2020Review
- Article
- Millisecond dynamics of an unlabeled amino acid transporter.Nature communications · 2020Article
- Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020Review
- Structural ensemble of a glutamate transporter homologue in lipid nanodisc environment.Nature communications · 2020Article
- A Perspective: Active Role of Lipids in Neurotransmitter Dynamics.Molecular neurobiology · 2020Review
- Article
- Lipid-Assisted Membrane Protein Folding and Topogenesis.The protein journal · 2019Review
- Perturbation of the yeast mitochondrial lipidome and associated membrane proteins following heterologous expression of Artemia-ANT.Scientific reports · 2018Article
- Effects of mixed proximal and distal topogenic signals on the topological sensitivity of a membrane protein to the lipid environment.Biochimica et biophysica acta. Biomembranes · 2017Article
- Article
- Dynamic membrane protein topological switching upon changes in phospholipid environment.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Fluorinated Aromatic Amino Acids Distinguish Cation-π Interactions from Membrane Insertion.The Journal of biological chemistry · 2015Article
- Structural and molecular determinants of glutamate transporter allosteric modulators.Molecular pharmacologyArticle
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The aspartate transporter from Pyrococcus horikoshii (GltPh) is a model for the structure of the SLC1 family of amino acid transporters. Crystal structures of GltPh provide insight into mechanisms of ion coupling and substrate transport; however, structures have been solved in the absence of a lipid bilayer so they provide limited information regarding interactions that occur between the protein and lipids of the membrane. Here, we investigated the effect of the lipid environment on aspartate transport by reconstituting GltPh into liposomes of defined lipid composition where the primary lipid is phosphatidylethanolamine (PE) or its methyl derivatives. We showed that the rate of aspartate transport and the transmembrane orientation of GltPh were influenced by the primary lipid in the liposomes. In PE liposomes, we observed the highest transport rate and showed that 85% of the transporters were orientated right-side out, whereas in trimethyl PE liposomes, 50% of transporters were right-side out, and we observed a 4-fold reduction in transport rate. Differences in orientation can only partially explain the lipid composition effect on transport rate. Crystal structures of GltPh revealed a tyrosine residue (Tyr-33) that we propose interacts with lipid headgroups during the transport cycle. Based on site-directed mutagenesis, we propose that a cation-π interaction between Tyr-33 and the lipid headgroups can influence conformational flexibility of the trimerization domain and thus the rate of transport. These results provide a specific example of how interactions between membrane lipids and membrane-bound proteins can influence function and highlight the importance of the role of the membrane in transporter function.
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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.