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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ryan, Renae M. Vandenberg, Robert J. Mcilwain, Benjamin C. |
| Description | Author Affiliation: McIlwain BC ( From the Transporter Biology Group, Discipline of Pharmacology and Bosch Institute, University of Sydney, Sydney, New South Wales 2006, Australia.); Vandenberg RJ ( From the Transporter Biology Group, Discipline of Pharmacology and Bosch Institute, University of Sydney, Sydney, New South Wales 2006, Australia.); Ryan RM ( From the Transporter Biology Group, Discipline of Pharmacology and Bosch Institute, University of Sydney, Sydney, New South Wales 2006, Australia renae.ryan@sydney.edu.au.) |
| 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. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 15 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-04-10 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amino Acid Transport System X-AG Genetics Archaeal Proteins Metabolism Lipid Bilayers Pyrococcus Horikoshii Chemistry Aspartic Acid Biological Transport Crystallography, X-Ray Kinetics Liposomes Models, Molecular Mutation Phosphatidylethanolamines Protein Binding Protein Structure, Tertiary Tyrosine Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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