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- W2947191850 abstract "Significance PSD-95 is a key scaffolding protein that is localized to the postsynaptic density of excitatory synapses where it regulates a wide variety of receptors, channels, and signaling molecules. However, the role of PSD-95 binding to the cell adhesion molecules, neuroligins, has been less clear. We now report that PSD-95 specifically regulates NLGN1 among the various neuroligin isoforms. In addition, we characterize a dynamic interaction between NLGN1 and PSD-95 that is regulated by the phosphorylation of NLGN1 by PKA. Phosphorylation on S839 of NLGN1 blocks PSD-95 binding, reduces surface and synaptic expression of NLGN1, and inhibits NLGN1-mediated enhancement of excitatory synaptic transmission." @default.
- W2947191850 created "2019-06-07" @default.
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- W2947191850 date "2019-05-28" @default.
- W2947191850 modified "2023-10-12" @default.
- W2947191850 title "PSD-95 binding dynamically regulates NLGN1 trafficking and function" @default.
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- W2947191850 doi "https://doi.org/10.1073/pnas.1821775116" @default.
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