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A novel mechanism of LTD involving liprin-α and LAR. Activation of mAChRs leads to a G-protein dependent mAChR-LTD that does not involve the canonical pathway (IP3 and PKC). The data can most simply be explained by GRIP acting as a targeting molecule that brings LAR and the GluA2 subunit of AMPARs into contact. This then enables LAR to dephosphorlyate a tyrosine residue (such as YGIESVKI on GluA2) which initiates the removal of the AMPAR from the synapse.
