| First Author | Matsuda K | Year | 2016 |
| Journal | Neuron | Volume | 90 |
| Issue | 4 | Pages | 752-67 |
| PubMed ID | 27133466 | Mgi Jnum | J:239574 |
| Mgi Id | MGI:5829167 | Doi | 10.1016/j.neuron.2016.04.001 |
| Citation | Matsuda K, et al. (2016) Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins. Neuron 90(4):752-67 |
| abstractText | Postsynaptic kainate-type glutamate receptors (KARs) regulate synaptic network activity through their slow channel kinetics, most prominently at mossy fiber (MF)-CA3 synapses in the hippocampus. Nevertheless, how KARs cluster and function at these synapses has been unclear. Here, we show that C1q-like proteins C1ql2 and C1ql3, produced by MFs, serve as extracellular organizers to recruit functional postsynaptic KAR complexes to the CA3 pyramidal neurons. C1ql2 and C1ql3 specifically bound the amino-terminal domains of postsynaptic GluK2 and GluK4 KAR subunits and the presynaptic neurexin 3 containing a specific sequence in vitro. In C1ql2/3 double-null mice, CA3 synaptic responses lost the slow, KAR-mediated components. Furthermore, despite induction of MF sprouting in a temporal lobe epilepsy model, KARs were not recruited to postsynaptic sites in C1ql2/3 double-null mice, leading to reduced recurrent circuit activities. C1q family proteins, broadly expressed, are likely to modulate KAR function throughout the brain and represent promising antiepileptic targets. |
