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  Different functional roles of arginine residues 39 and 61 and tyrosine residue 98 in transport and channel mode of the glutamate transporter EAAC1

Zhu, Y., Vasilets, L., Fei, J., Guo, L., & Schwarz, W. (2004). Different functional roles of arginine residues 39 and 61 and tyrosine residue 98 in transport and channel mode of the glutamate transporter EAAC1. Biochimica et Biophysica Acta: BBA, 1665, 20-28. doi:10.1016/j.bbamem.2004.06.007.

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 Creators:
Zhu, Yani1, Author           
Vasilets, L.A.2, Author
Fei, J.1, Author           
Guo, L.2, Author
Schwarz, Wolfgang1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2External Organizations, ou_persistent22              

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 Abstract: The excitatory amino acid transporter EAAC1 is an electrogenic Na+ - and K+ -gradient-driven transporter. In addition, the transporter mediates in the presence of Na+ and glutamate an anion conductance uncoupled from the transport of the glutamate. The first two N-terminal domains, important for forming the conductance mode, are extracellularly bordered by positively charged arginine residues, R39 and R61, being completely conserved throughout the transporter family. Also the conserved tyrosine residue Y98 could be important for Cl- conductance. We have investigated, by measurements of glutamate uptake and glutamate-induced currents, the effects of mutation of the arginines and the tyrosine to alanine. The mutation R39A hardly affects transport and channel mode. The mutation R61A, on the other hand, reduces the activity of transport but stimulates the channel conductance. In addition, the apparent Km values for glutamate uptake and for the glutamate-activated current are reduced. Glutamate stimulation of current seems to be associated with a voltage-dependent step, and the apparent valence of charge moved during binding is reduced in the R61A mutant. The mutation Y98A leads to reduced function with reduced apparent Km value for glutamate, and with strong reduction of the selectivity ration between NO3- and Cl- of the conductance mode.

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Language(s): eng - English
 Dates: 2004
 Publication Status: Issued
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 221038
DOI: 10.1016/j.bbamem.2004.06.007
 Degree: -

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Title: Biochimica et Biophysica Acta : BBA
  Other : Biochimica et Biophysica Acta (BBA) - Biomembranes
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1665 Sequence Number: - Start / End Page: 20 - 28 Identifier: Other: 1879-2642
CoNE: https://pure.mpg.de/cone/journals/resource/18792642