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Protein has unique effects in neural connections related to information processing Date: October 9, 2018 Source: Picower Institute at MIT Summary: The protein SAP102, which is implicated in intellectual disability, appears to play a key and potentially unique role in regulating the form of postsynaptic AMPAR receptor currents in the brain, a new study finds. Share: Our cognitive abilities come down to how well the connections, or synapses, between our brain cells transmit signals. A new study by researchers at MIT's Picower Institute for Learning and Memory digs deep into the molecular mechanisms that enable synaptic transmission to show the distinct role of a protein that when mutated has been linked to causing intellectual disability. The key protein, called SAP102, is one of four members of a family of proteins, called PSD-MAGUKs, that regulate the transport and placement of key receptors called AMPARs on the receiving end of a synapse. But how each member of the family works, for instance as the brain progresses through development to maturity, is not well understood. The new study in the Journal of Neurophysiology shows that SAP102 and other family members like PSD-95, work in different ways, a feature whose evolution may have contributed to the greater cognitive capacity of mammals and other vertebrates. Current affairs Specifically, the scientists found that the proteins distinctly affected how quickly electrical currents lost strength in postsynaptic cells, or neurons. In one key set of experiments in rats in a region of the brain called the hippocampus, the researchers showed that while knocking out PSD-95 causes a reduction in AMPAR current frequency and amplitude, they could restore those by replacing PSD-95 with a different form, PSD-95alpha, or with SAP102. They did these manipulations by using a virus to make the swap, a technique called molecular replacement that Xu has developed. But the two proteins are not merely interchangeable. That timing difference made by SAP102 could make an important difference in how synapses operate to affect cognition. Protein partner In another set of experiments, the team showed that SAP102 uniquely depends on another protein called CNIH-2. Knocking the protein down on its own didn't affect AMPAR currents, but when they knocked down CNIH-2 in the context of replacing PSD-95 with PSD-95alpha or SAP102, the researchers found that SAP102 could no longer restore the currents. Meanwhile, knocking down CNIH-2 had no effect on PSD-95alpha's rescue of AMPAR currents. In all the findings suggest that the diversity of AMPAR regulation leads to cognitively consequential differences in current timing at synapses.
