The scaffolding molecule MAGI-1 causes changes in habituation kinetics in c. elegans by interacting with this protein through an intracellular domain involved in localization to the ventral cord.
The scaffolding molecule MAGI-1 causes changes in habituation kinetics in c. elegans by interacting with this protein through an intracellular domain involved in localization to the ventral cord. Its insertion requires CaMKII phosphorylation of TARP proteins, including stargazin. Insertion of glycosylation sites into genes coding for it shows that it has extracellular N and intracellular C termini with a flip/flop region N-terminal to TMD4 that controls desensitization. Blocked by CNQX and DNQX, as well as the broad-spectrum kynurenic acid, its agonists include homocysteate and quis. All but its R2 isoform are permeable to calcium, and other receptors in this tetramer's family include the kainate and NMDA receptors. Phosphorylated by CaM kinase, its localization is crucial for long-term potentiation. FTP, name this glutamate receptor responsible for the bulk of the excitatory transmission in the brain, given a four-letter acronym.
The scaffolding molecule MAGI-1 causes changes in habituation kinetics in c. elegans by interacting with this protein through an intracellular domain involved in localization to the ventral cord.
AMPA receptor (or alpha-amino-3-hydroxy-5-methyl-4-isoxazoleproprionic acid receptor)