Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains
| Autor: | Sagar Chittori, Carla Glasser, Peter Schuck, Suvendu Lomash, Mark L. Mayer, Huaying Zhao |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
QH301-705.5 Science Protein subunit Structural Biology and Molecular Biophysics Kainate receptor Gating AMPA receptor protein interactions General Biochemistry Genetics and Molecular Biology Protein–protein interaction 03 medical and health sciences Receptors Kainic Acid None Humans Receptors AMPA Biology (General) Receptor Ion channel General Immunology and Microbiology Chemistry Protein Stability General Neuroscience General Medicine Kinetics Protein Subunits 030104 developmental biology HEK293 Cells Biochemistry glutamate receptors Biophysics Medicine Thermodynamics Metabotropic glutamate receptor 2 Protein Multimerization Ultracentrifugation sedimentation velocity Research Article Neuroscience |
| Zdroj: | eLife eLife, Vol 6 (2017) |
| ISSN: | 2050-084X |
| Popis: | Ion conductivity and the gating characteristics of tetrameric glutamate receptor ion channels are determined by their subunit composition. Competitive homo- and hetero-dimerization of their amino-terminal domains (ATDs) is a key step controlling assembly. Here we measured systematically the thermodynamic stabilities of homodimers and heterodimers of kainate and AMPA receptors using fluorescence-detected sedimentation velocity analytical ultracentrifugation. Measured affinities span many orders of magnitude, and complexes show large differences in kinetic stabilities. The association of kainate receptor ATD dimers is generally weaker than the association of AMPA receptor ATD dimers, but both show a general pattern of increased heterodimer stability as compared to the homodimers of their constituents, matching well physiologically observed receptor combinations. The free energy maps of AMPA and kainate receptor ATD dimers provide a framework for the interpretation of observed receptor subtype combinations and possible assembly pathways. |
| Databáze: | OpenAIRE |
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