Abstract
Synaptic plasticity, the neural substrate of learning and memory, is essential throughout life and its decline impedes healthy aging. Phosphorylation-dependent changes in the function and trafficking of AMPA-type glutamate receptors drive synaptic plasticity, but the molecular mechanisms are poorly understood. To determine how phosphorylation of the intracellular C-tails of AMPA receptors and their auxiliary proteins modulates their structure and function we will combine quantitative cross-linking coupled to mass spectrometry and patch-clamp electrophysiology. This novel combination of interdisciplinary approaches will provide insight into the key protein-protein interactions that underlie a fundamental process responsible for synaptic plasticity.
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