@article{b51a52a29c2c4618af01cbdb3ef5e099,
title = "Distinct Subunit Domains Govern Synaptic Stability and Specificity of the Kainate Receptor",
abstract = "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.",
author = "Christoph Straub and Yoav Noam and Toshihiro Nomura and Miwako Yamasaki and Dan Yan and Fernandes, {Herman B.} and Ping Zhang and Howe, {James R.} and Masahiko Watanabe and Anis Contractor and Susumu Tomita",
note = "Funding Information: The authors thank the members of S.T.{\textquoteright}s and A.C.{\textquoteright}s labs for helpful discussions. We thank Dr. Megumi Morimoto-Tomita for generating various reagents, Dr. S.F. Heinemann (Salk Institute), Dr. Peter Seeburg (Max Planck Institute), Deltagen, Genentech, KOMP for generating each of GluK2/4/5 knockouts, GluA1 knockout, Neto2 knockout, Neto1 knockout mice, and the Jackson laboratory and MMRRC for maintaining GluK2, GluK5, Neto2 knockout, and stargazer mice. Parts of this study were supported by NIH/NIMH R01 MH085080 and the Yale fund (S.T.) and NIH/NIMH R01 MH099114 (A.C.). M.W. is supported by Grants-in-Aid for Scientific Research provided by the Ministry of Education, Culture, Sports, Science and Technology of Japan. C.S. was supported by a Boehringer-Ingelheim Fonds PhD fellowship, and Y.N was supported by NIH/NINDS NRSA post-doctoral fellowship (F32 NS093952). Publisher Copyright: {\textcopyright} 2016",
year = "2016",
month = jul,
day = "12",
doi = "10.1016/j.celrep.2016.05.093",
language = "English (US)",
volume = "16",
pages = "531--544",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "2",
}