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TitleStructural and compositional diversity in the kainate receptor family.
Journal, issue, pagesCell Rep, Vol. 37, Issue 4, Page 109891, Year 2021
Publish dateOct 26, 2021
AuthorsPurushotham Selvakumar / Joon Lee / Nandish Khanra / Changhao He / Hermany Munguba / Lisa Kiese / Johannes Broichhagen / Andreas Reiner / Joshua Levitz / Joel R Meyerson /
PubMed AbstractThe kainate receptors (KARs) are members of the ionotropic glutamate receptor family and assemble into tetramers from a pool of five subunit types (GluK1-5). Each subunit confers distinct functional ...The kainate receptors (KARs) are members of the ionotropic glutamate receptor family and assemble into tetramers from a pool of five subunit types (GluK1-5). Each subunit confers distinct functional properties to a receptor, but the compositional and stoichiometric diversity of KAR tetramers is not well understood. To address this, we first solve the structure of the GluK1 homomer, which enables a systematic assessment of structural compatibility among KAR subunits. Next, we analyze single-cell RNA sequencing data, which reveal extreme diversity in the combinations of two or more KAR subunits co-expressed within the same cell. We then investigate the composition of individual receptor complexes using single-molecule fluorescence techniques and find that di-heteromers assembled from GluK1, GluK2, or GluK3 can form with all possible stoichiometries, while GluK1/K5, GluK2/K5, and GluK3/K5 can form 3:1 or 2:2 complexes. Finally, using three-color single-molecule imaging, we discover that KARs can form tri- and tetra-heteromers.
External linksCell Rep / PubMed:34706237 / PubMed Central
MethodsEM (single particle)
Resolution4.6 Å
Structure data

EMDB-23542, PDB-7lvt:
Structure of full-length GluK1 with L-Glu
Method: EM (single particle) / Resolution: 4.6 Å

Source
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / ion channel / glutamate receptor / kainate receptor

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