GRIK2
Gene Ontology Biological Process
- glutamate receptor signaling pathway [TAS]
- ion transmembrane transport [IBA]
- ionotropic glutamate receptor signaling pathway [IBA]
- positive regulation of synaptic transmission [IMP]
- regulation of short-term neuronal synaptic plasticity [IMP]
- regulation of synaptic transmission [IDA]
- synaptic transmission [TAS]
- synaptic transmission, glutamatergic [IBA]
- transport [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
GRIK2
Gene Ontology Biological Process
- glutamate receptor signaling pathway [TAS]
- ion transmembrane transport [IBA]
- ionotropic glutamate receptor signaling pathway [IBA]
- positive regulation of synaptic transmission [IMP]
- regulation of short-term neuronal synaptic plasticity [IMP]
- regulation of synaptic transmission [IDA]
- synaptic transmission [TAS]
- synaptic transmission, glutamatergic [IBA]
- transport [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains.
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 ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| GRIK2 GRIK2 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| GRIK2 GRIK2 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | Low | - | BioGRID | - | |
| GRIK2 GRIK2 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - | |
| GRIK2 GRIK2 | Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps. | Low | - | BioGRID | - |
Curated By
- BioGRID