Manage your Funding Opportunities

Pierre Moenne-Loccoz Institute of Environmental Health

Empty picture place holder

Pierre Moenne-Loccoz


Manage your Funding

Scopus Publication Detail

The publication detail shows the title, authors (with indicators showing other profiled authors), information on the publishing organization, abstract and a link to the article in Scopus. This abstract is what is used to create the fingerprint of the publication.

Opposite movement of the external gate of a glutamate transporter homolog upon binding cotransported sodium compared with substrate

Paul J. Focke; Pierre Moenne-Loccoz; H.Peter Larsson

(Profiled Author: Pierre Moenne-Loccoz)

Journal of Neuroscience. 2011;31(16):6255-6262.


Recently, a new model for glutamate uptake by glutamate transporters was proposed based on crystal structures of the bacterial glutamate transporter homolog GltPh.It was proposed that hairpin two (HP2) functions as the extra cellular gate and that Na + and glutamate binding closes HP2, thereby allowing for the translocation of the glutamate binding pocket across the membrane. However, the conformation of HP2 in the apo state and the Na + bound state is unknown. We here use double site-directed spin-labeling electron paramagnetic resonance spectroscopy on the bacterial transporter GltPh from Pyrococcus horikoshi to examine conformational changes in HP2. Surprisingly, the cotransported substrates Na + and as partate induce opposite movements of HP2. We find that in the apo state, HP2 is in a similar conformation as in the as partate-bound closed state. Na + binding to the apo state opens HP2, whereas the subsequent binding of as partate closes HP2. Our findings show that Na + binding opens and stabilizes the extra cellular gate, thereby allowing for amino acid substrate binding. In contrast, in the absence of Na + and as partate, HP2 closes, suggesting a potential mechanism for the translocation of the empty binding pocket necessary to complete the transport cycle. The finding that physiological Na + concentrations stabilize the open HP2 state would ensure that the outward-facing conformation of the transporter is maintained in physiological solutions and that glutamate transporters are ready to quickly bind glutamate released from glutamatergic synapses. © 2011the authors.

PMID: 21508248     PMCID: PMC3096012    

Scientific Context

This section shows information related to the publication - computed using the fingerprint of the publication - including related publications, related experts with fingerprints representing significant amounts of overlap between their fingerprint and this publication. The red dots indicate whether those experts or terms appear within the publication, thereby showing potential and actual connections.

Related Publications

Related Topics

Appears in this Publication Appears in this Document

Related Experts

Author of this Publication Author of this Document