Fig. 2

AMPAR and its associated scaffold proteins whose palmitoylation contributes to the modulation of spine morphology. The figure shows that several associated scaffold proteins of the AMPAR GluA1/2 and GluA2/3 heterotetramers (the major combinations of functional AMPARs in nervous system) undergo palmitoylation in the postsynaptic side of the excitatory synapses to regulate AMPAR membrane trafficking and postsynaptic architecture. Noteworthy, Ankyrin-G was shown to partially colocalize with GluA1 puncta perisynaptically in the spine head but the interaction between Ankyrin-G and GluA1 seems to be indirect and could be mediated by multiple proteins [244]. Palmitoylation of these proteins appears to play important roles in regulating their membrane localization and affects AMPAR trafficking on the postsynaptic membrane. It also contributes to spine structure modulation through various signaling pathways, which are described in this chapter. TARP: transmembrane AMPA receptor regulatory protein. One squiggle denotes one or more palmitoyl chains attached to the targeted protein. PSD-95 line icon denotes several PSD-95 molecules