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AMPA receptors are a subfamily of ionotropic glutamate receptors and play a crucial role in fast signal transduction in the brain. Although AMPA receptors can exert their basic function, i.e., fluxing ions into the cell upon binding of glutamate, on their own, many other proteins are involved in the fine tuning of this process. Most of these proteins are important for transporting the AMPA receptors to their correct destination when they are needed, but also for removing them when they are not needed any more. The discovery of a family of six small membrane proteins that are also involved in this regulation of transport, but in addition directly change the functional properties of AMPA receptors, was a surprising achievement. In particular, these transmembrane AMPA receptor regulatory proteins (TARPs) boost the glutamate-induced signal by increasing the opening time of the AMPA receptor channel. To understand the function of AMPA receptors, it is important to understand this mechanism. We are particularly interested in characterising the different impacts of the different TARPs on AMPA receptors and investigate the interactions that form the basis of this differential modulation.
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