The Noelin family of secreted proteins bind to the external portion of AMPA glutamate receptors and stabilize them on the neuronal cellular membrane, a process necessary for transmission of full-strength signals between neurons, according to a study in mice from the National Eye Institute (NEI) and the University of Freiberg, Germany. Without this external, stabilizing protein network, the AMPA receptors are no longer retained at the synapse, leading to weak, short-lived synaptic signals.
The findings not only provide insight into processes such as learning and memory but also the development of blinding conditions like glaucoma. The study was published in the journal"This study shows that Noelins have a crucial job in supporting synapse function in the brain and other neural tissues like the eye's retina," said Stanislav Tomarev, Ph.D., chief of NEI's Section on Retinal Ganglion Cell Biology and co-senior author of the report.
The presynaptic"sending" cell emits glutamate, which travels across the synaptic cleft and is sensed by glutamate receptors on the postsynaptic"receiving" cell. These glutamate receptors are; when the channels sense glutamate, they open, generating a new neuronal signal within the postsynaptic cell. In order to generate a strong signal, sufficient receptors must be present in the correct location of the cell's surface at the synapse.
The researchers first took mouse brain tissue, and isolated cellular membranes and their attached proteins. Using mass spectroscopy and specialized analytic techniques, the team worked out which proteins were associating with AMPA receptors in these membranes.
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