Mutation of an amino acid residue influencing potassium coupling in the glutamate transporter GLT-1 induces obligate exchange
MP Kavanaugh, A Bendahan, N Zerangue… - Journal of Biological …, 1997 - ASBMB
Glutamate transporters maintain low synaptic concentrations of neurotransmitter by coupling
uptake to flux of other ions. After cotransport of glutamic acid with Na+, the cycle is
completed by countertransport of K+. We have identified an amino acid residue (glutamate
404) influencing ion coupling in a domain of the transporter implicated previously in kainate
binding. Mutation of this residue to aspartate (E404D) prevents both forward and reverse
transport induced by K+. Sodium-dependent transmitter exchange and a transporter …
uptake to flux of other ions. After cotransport of glutamic acid with Na+, the cycle is
completed by countertransport of K+. We have identified an amino acid residue (glutamate
404) influencing ion coupling in a domain of the transporter implicated previously in kainate
binding. Mutation of this residue to aspartate (E404D) prevents both forward and reverse
transport induced by K+. Sodium-dependent transmitter exchange and a transporter …
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