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

18Citations
Citations of this article
9Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free