| First Author | Straub C | Year | 2016 |
| Journal | Cell Rep | Volume | 16 |
| Issue | 2 | Pages | 531-544 |
| PubMed ID | 27346345 | Mgi Jnum | J:238521 |
| Mgi Id | MGI:5822969 | Doi | 10.1016/j.celrep.2016.05.093 |
| Citation | Straub C, et al. (2016) Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor. Cell Rep 16(2):531-44 |
| abstractText | Synaptic communication between neurons requires the precise localization of neurotransmitter receptors to the correct synapse type. Kainate-type glutamate receptors restrict synaptic localization that is determined by the afferent presynaptic connection. The mechanisms that govern this input-specific synaptic localization remain unclear. Here, we examine how subunit composition and specific subunit domains contribute to synaptic localization of kainate receptors. The cytoplasmic domain of the GluK2 low-affinity subunit stabilizes kainate receptors at synapses. In contrast, the extracellular domain of the GluK4/5 high-affinity subunit synergistically controls the synaptic specificity of kainate receptors through interaction with C1q-like proteins. Thus, the input-specific synaptic localization of the native kainate receptor complex involves two mechanisms that underlie specificity and stabilization of the receptor at synapses. |
