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Abstract
The scaffold protein PSD-95 promotes the maturation and strengthening of excitatory synapses, functions that require proper localization of PSD-95 in the postsynaptic density (PSD). Here we report that phosphorylation of ser-295 enhances the synaptic accumulation of PSD-95 and the ability of PSD-95 to recruit surface AMPA receptors and potentiate excitatory postsynaptic currents. We present evidence that a Rac1-JNK1 signaling pathway mediates ser-295 phosphorylation and regulates synaptic content of PSD-95. Ser-295 phosphorylation is suppressed by chronic elevation, and increased by chronic silencing, of synaptic activity. Rapid dephosphorylation of ser-295 occurs in response to NMDA treatment that causes chemical long-term depression (LTD). Overexpression of a phosphomimicking mutant (S295D) of PSD-95 inhibited NMDA-induced AMPA receptor internalization and blocked the induction of LTD. The data suggest that synaptic strength can be regulated by phosphorylation-dephosphorylation of ser-295 of PSD-95 and that synaptic depression requires the dephosphorylation of ser-295.
Translated title of the contribution | Synaptic accumulation of PSD-95 and synaptic function regulated by phosphorylation of serine-295 of PSD-95 |
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Original language | English |
Pages (from-to) | 488 - 502 |
Number of pages | 15 |
Journal | Neuron |
Volume | 56 |
DOIs | |
Publication status | Published - Nov 2007 |
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SYNAPTIC TRANSMISSION IN HUMAN ES CELL DERIVED NEURONS: A POTENTIAL REPLACEMENT MODEL IN THE CNS
Cho, K. (Principal Investigator)
1/11/07 → 1/08/10
Project: Research