Stabilization of Ca2+-permeable AMPA receptors at perisynaptic sites by GluR1-S845 phosphorylation.

@article{He2009StabilizationOC,
  title={Stabilization of Ca2+-permeable AMPA receptors at perisynaptic sites by GluR1-S845 phosphorylation.},
  author={Kaiwen He and Lihua Song and Laurel W Cummings and Jonathan Wade Goldman and Richard L. Huganir and Hey-Kyoung Lee},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 47},
  pages={20033-8}
}
AMPA receptor (AMPAR) channel properties and function are regulated by its subunit composition and phosphorylation. Certain types of neural activity can recruit Ca(2+)-permeable (CP) AMPARs, such as GluR1 homomers, to synapses likely via lateral diffusion from extrasynaptic sites. Here we show that GluR1-S845 phosphorylation can alter the subunit composition of perisynaptic AMPARs by providing stability to GluR1 homomers. Using mice specifically lacking phosphorylation of the GluR1-S845 site… CONTINUE READING
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