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Updated: Jul 13, 2026

A High-content Assay for Monitoring AMPA Receptor Trafficking
Published on: January 28, 2019
Rigidity of the subunit interfaces of the trimeric glutamate transporter GltT during translocation
Maarten Groeneveld1, Dirk-Jan Slotboom
1Department of Biochemistry, University of Groningen, Groningen Biomolecular Science and Biotechnology Institute, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Abstract:
Glutamate transporters are trimeric membrane proteins in which each protomer contains a separate translocation path. To determine whether structural rearrangements take place at the subunit interfaces during transport, intersubunit disulfide bridges were introduced in the bacterial transporter GltT. None of the intersubunit cross-links, which had been designed across the entire interface, affected the glutamate transport activity, indicating that the subunit interfaces are rigid during turnover.
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