Structural and functional insights into transmembrane AMPA receptor regulatory protein complexes
| Autor: | Edward C. Twomey, Alexander I. Sobolevsky, Maria V. Yelshanskaya |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Physiology Protein subunit Reviews Glutamic Acid Context (language use) Review AMPA receptor Neurotransmission Synaptic Transmission 03 medical and health sciences 0302 clinical medicine Animals Humans Receptors AMPA Ion channel Neurons Chemistry musculoskeletal neural and ocular physiology Glutamate receptor Brain Membrane Proteins Cell biology Protein Transport 030104 developmental biology nervous system Claudins Excitatory postsynaptic potential Ionotropic glutamate receptor 030217 neurology & neurosurgery |
| Zdroj: | The Journal of General Physiology |
| ISSN: | 1540-7748 0022-1295 |
| DOI: | 10.1085/jgp.201812264 |
| Popis: | Twomey et al. examine recent structural and functional data that have provided insight into AMPA receptor modulation by TARPs. Fast excitatory neurotransmission is mediated by the α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) subtype of ionotropic glutamate receptor (AMPAR). AMPARs initiate depolarization of the postsynaptic neuron by allowing cations to enter through their ion channel pores in response to binding of the neurotransmitter glutamate. AMPAR function is dramatically affected by auxiliary subunits, which are regulatory proteins that form various complexes with AMPARs throughout the brain. The most well-studied auxiliary subunits are the transmembrane AMPAR regulatory proteins (TARPs), which alter the assembly, trafficking, localization, kinetics, and pharmacology of AMPARs. Recent structural and functional studies of TARPs and the TARP-fold germ cell-specific gene 1-like (GSG1L) subunit have provided important glimpses into how auxiliary subunits regulate the function of synaptic complexes. In this review, we put these recent structures in the context of new functional findings in order to gain insight into the determinants of AMPAR regulation by TARPs. We thus reveal why TARPs display a broad range of effects despite their conserved modular architecture. |
| Databáze: | OpenAIRE |
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