Background: Glutamate transporters gate anion conductance and structures of homologues are available. Results: Disulfide cross-linking of transport and trimerization domains leaves the anion conductance intact. Conclusion: The anion conducting conformation of brain glutamate transporters is associated with a limited inward movement of the transport domain. Significance: The new insights into ion conducting modes may be relevant for other transporters. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Shabaneh, M., Rosental, N., & Kanner, B. I. (2014). Disulfide cross-linking of transport and trimerization domains of a neuronal glutamate transporter restricts the role of the substrate to the gating of the anion conductance. Journal of Biological Chemistry, 289(16), 11175–11182. https://doi.org/10.1074/jbc.M114.550277
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