Abstract: |
The clustering of neurotransmitter receptors at the postsynaptic terminals is a critical requirement for efficient neurotransmission and neuronal communication. This process is facilitated by adaptor proteins, which bridge the postsynaptic receptors and the underlying cytoskeleton. One such molecule, the GABAA receptor-associated protein, GABARAP, was identified as a potential linker between GABAA receptors and microtubules. GABARAP belongs to an expanding family of proteins that are implicated in a variety of intracellular transport processes. GABARAP has been shown to interact with myriad binding partners, including the γ2 subunit of the GABAA receptor, tubulin and microtubules, the N-ethyl maleimide sensitive factor, gephyrin, and the transferin receptor. The recent determination of the GABARAP crystal structure has revealed individual GABARAP domains, motifs, and surface regions involved in specific protein-protein interactions. Currently, a more general role is emerging for GABARAP, including shipping GABAA receptors to and from the cell surface, organizing them into postsynaptic clusters, and regulating the steady-state receptor density. |
Keywords: |
unclassified drug; review; nonhuman; animals; steady state; protein protein interaction; protein binding; intracellular transport; protein transport; adaptor proteins, signal transducing; crystal structure; models, molecular; protein structure, tertiary; receptor affinity; tubulin; microtubule; cytoskeleton; synapses; adaptor protein; microtubule-associated proteins; receptor protein; neurotransmission; gabarap; 4 aminobutyric acid a receptor; synaptogenesis; receptors, gaba-a; synapse formation; humans; human; priority journal; gabaa receptors; receptor trafficking; 4 aminobutyric acid a receptor associated protein; gephyrin; neurotransmitter receptor; postsynaptic receptor; postsynaptic potential; receptors, glycine
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