Kainate receptor post-translational modifications differentially regulate association with 4.1N to control activity-dependent receptor endocytosis.

@article{Copits2013KainateRP,
  title={Kainate receptor post-translational modifications differentially regulate association with 4.1N to control activity-dependent receptor endocytosis.},
  author={Bryan A. Copits and Geoffrey T Swanson},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 13},
  pages={8952-65}
}
Kainate receptors exhibit a highly compartmentalized distribution within the brain; however, the molecular and cellular mechanisms that coordinate their expression at neuronal sites of action are poorly characterized. Here we report that the GluK1 and GluK2 kainate receptor subunits interact with the spectrin-actin binding scaffolding protein 4.1N through a membrane-proximal domain in the C-terminal tail. We found that this interaction is important for the forward trafficking of GluK2a… CONTINUE READING

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Synaptic homeostasis requires the membrane-proximal carboxy tail of GluA 2

Samantha G. Ancona Esselmanna, Javier Díaz-Alonsob, Jonathan M. Levya, Michael A. Bembenb, Roger A. Nicollb
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A proteomic analysis reveals the interaction of GluK1 ionotropic kainate receptor subunits with Go proteins.

The Journal of neuroscience : the official journal of the Society for Neuroscience • 2015
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