Ubiquitin proteasome system–mediated, neuronal activity–dependent protein turnover at synapses often occurs in an ensemble fashion where a group or groups of postsynaptic density (PSD) proteins are degraded together in a homeostatic response. This study shows that the synaptic level of the PSD scaffolding protein called GKAP (also known as SAPAP1) is bidirectionally regulated in a homeostatic fashion and is mediated by differential phosphorylation by CaM kinase II isoforms.
- Seung Min Shin
- Nanyan Zhang
- Sang H Lee
