English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

Expression and transport function of the glutamate transporter EAAC1 in Xenopus oocytes is regulated by syntaxin 1A

MPS-Authors
/persons/resource/persons137961

Zhu,  Yani
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Max-Planck Guest Laboratory at the Institute of Biochemistry and Cell Biology, CAS, Shanghai, China;
Laboratory of Molecular Cell Biology, Institute of Biochemistry and Cell Biology, CAS, Shanghai, China;

/persons/resource/persons137890

Schwarz,  Wolfgang
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Max-Planck Guest Laboratory at the Institute of Biochemistry and Cell Biology, CAS, Shanghai, China;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Zhu, Y., Fei, J., & Schwarz, W. (2005). Expression and transport function of the glutamate transporter EAAC1 in Xenopus oocytes is regulated by syntaxin 1A. Journal of Neuroscience Research, 79(4), 503-508. doi:10.1002/jnr.20385.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-DA07-C
Abstract
The function of several membrane proteins is regulated by interaction with the SNARE protein syntaxin 1A; this includes regulation of GAT1, the transporter for the dominating inhibitory neurotransmitter gamma-aminobutyric acid (GABA). Here we demonstrate that also EAAC1, the transporter for the dominating excitatory neurotransmitter, is down-regulated by interaction with syntaxin 1A. This is shown by coexpression of EAAC1 and syntaxin 1A in Xenopus oocytes. Total EAAC1 expression is not significantly affected by the coexpression of syntaxin 1A, but more proteins become targeted to the membrane as demonstrated by biotinylation. Colocalization by coimmunoprecipitation suggests direct interaction between the two proteins. In contrast to the number of transporters, the glutamate transport activity becomes reduced, and even stronger inhibition is observed for the EAAC1-mediated conductance uncoupled from glutamate translocation. We conclude that the interaction of syntaxin 1A with EAAC1 particularly disrupts the structure of the conductance pathway of EAAC1.