Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins.
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-li...
| Huvudupphovsmän: | , , , , , , , , , , , , , , , |
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| Materialtyp: | Journal article |
| Språk: | English |
| Publicerad: |
Elsevier
2016
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| _version_ | 1826269450228203520 |
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| author | Matsuda, K Budisantoso, T Mitakidis, N Sugaya, Y Miura, E Kakegawa, W Yamasaki, M Konno, K Uchigashima, M Abe, M Watanabe, I Kano, M Watanabe, M Sakimura, K Aricescu, A Yuzaki, M |
| author_facet | Matsuda, K Budisantoso, T Mitakidis, N Sugaya, Y Miura, E Kakegawa, W Yamasaki, M Konno, K Uchigashima, M Abe, M Watanabe, I Kano, M Watanabe, M Sakimura, K Aricescu, A Yuzaki, M |
| author_sort | Matsuda, K |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T21:25:14Z |
| format | Journal article |
| id | oxford-uuid:42e1f818-ae2f-40d1-b09f-2cadf72ce3ba |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:25:14Z |
| publishDate | 2016 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:42e1f818-ae2f-40d1-b09f-2cadf72ce3ba2022-03-26T14:52:01ZTranssynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:42e1f818-ae2f-40d1-b09f-2cadf72ce3baEnglishSymplectic Elements at OxfordElsevier2016Matsuda, KBudisantoso, TMitakidis, NSugaya, YMiura, EKakegawa, WYamasaki, MKonno, KUchigashima, MAbe, MWatanabe, IKano, MWatanabe, MSakimura, KAricescu, AYuzaki, MPostsynaptic 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. |
| spellingShingle | Matsuda, K Budisantoso, T Mitakidis, N Sugaya, Y Miura, E Kakegawa, W Yamasaki, M Konno, K Uchigashima, M Abe, M Watanabe, I Kano, M Watanabe, M Sakimura, K Aricescu, A Yuzaki, M Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins. |
| title | Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins. |
| title_full | Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins. |
| title_fullStr | Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins. |
| title_full_unstemmed | Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins. |
| title_short | Transsynaptic Modulation of Kainate Receptor Functions by C1q-like Proteins. |
| title_sort | transsynaptic modulation of kainate receptor functions by c1q like proteins |
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