ArticleFrontiers in molecular neuroscience2026
Proline-directed phosphorylation and prolyl isomerization oppose each other to regulate PSD-95 ubiquitination and excitatory synaptic plasticity.
Article in Frontiers in molecular neuroscience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
PSD-95 is a key scaffolding protein in excitatory synapses, playing a critical role in stabilizing synaptic receptors. Post-translational modifications such as phosphorylation and ubiquitination have been shown to regulate PSD-95's localization and stability. Threonine 19 (T19) phosphorylation has emerged as a key phosphorylation site involved in NMDAR-dependent LTD; however, its role in PSD-95 ubiquitination is unknown. This study aims to elucidate the role of T19 phosphorylation in regulating PSD-95 ubiquitination, and whether the peptidyl prolyl isomerase 1 (Pin1), a known phospho-T19 binding protein, modifies this process. Our results support the idea that T19 and S25 phosphorylation positively regulate PSD-95 ubiquitination. Furthermore, we found that the Pin1 binding to S25 lowered the phosphorylation state of T19 and prevented PSD-95 ubiquitination. Finally, whole-cell recordings show that GSK3 overexpression depressed baseline synaptic transmission and partially blocked NMDAR-LTD, and both effects were rescued by Pin1 overexpression. Together, these findings provide insights into the molecular mechanisms regulating PSD-95 stability at synapses.
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