AKAP150 Palmitoylation Regulates Synaptic Incorporation of Ca2+-Permeable AMPA Receptors to Control LTP.
作者： Alicia M. Purkey , Kevin M. Woolfrey , Kevin C. Crosby , Dominik G. Stich , Wallace S. Chick
DOI: 10.1016/J.CELREP.2018.09.085
关键词: Synaptic plasticity 、 Phosphorylation 、 Postsynaptic density 、 AMPA receptor 、 Cell biology 、 Long-term potentiation 、 Palmitoylation 、 Glutamate receptor 、 Chemistry 、 Endosome
摘要: Ca2+-permeable AMPA-type glutamate receptors (CP-AMPARs) containing GluA1 but lacking GluA2 subunits contribute to multiple forms of synaptic plasticity, including long-term potentiation (LTP), mechanisms regulating CP-AMPARs are poorly understood. A-kinase anchoring protein (AKAP) 150 scaffolds kinases and phosphatases regulate phosphorylation trafficking, trafficking AKAP150 itself is modulated by palmitoylation on two Cys residues. Here, we developed a palmitoylation-deficient knockin mouse show that regulates CP-AMPAR incorporation at hippocampal synapses. Using biochemical, super-resolution imaging, electrophysiological approaches, found promotes localization recycling endosomes the postsynaptic density (PSD) limit basal incorporation. In addition, required for LTP induced weaker stimulation recruits synapses not stronger GluA2-containing AMPARs. Thus, controls its subcellular maintain proper activity-dependent regulation AMPAR subunit composition.
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