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Background  Sustained changes in network activity cause homeostatic synaptic plasticity in part by altering the postsynaptic accumulation of N-methyl-D-aspartate receptors (NMDAR) and α-amino-3-hydroxyle-5-methyl-4-isoxazolepropionic acid receptors (AMPAR), which are primary mediators of excitatory synaptic transmission. A key trafficking modulator of NMDAR and AMPAR is STriatal-Enriched protein tyrosine Phosphatase (STEP 61 ) that opposes synaptic strengthening through dephosphorylation of NMDAR subunit GluN2B and AMPAR subunit GluA2. However, the role of STEP 61  in homeostatic synaptic plasticity is unknown.    Findings  We demonstrate here that prolonged activity blockade leads to synaptic scaling, and a concurrent decrease in STEP 61  level and activity in rat dissociated hippocampal cultured neurons. Consistent with STEP 61  reduction, prolonged activity blockade enhances the tyrosine phosphorylation of GluN2B and GluA2 whereas increasing STEP 61  activity blocks this regulation and synaptic scaling. Conversely, prolonged activity enhancement increases STEP 61  level and activity, and reduces the tyrosine phosphorylation and level of GluN2B as well as GluA2 expression in a STEP 61 –dependent manner.    Conclusions  Given that STEP 61 -mediated dephosphorylation of GluN2B and GluA2 leads to their internalization, our results collectively suggest that activity-dependent regulation of STEP 61  and its substrates GluN2B and GluA2 may contribute to homeostatic stabilization of excitatory synapses.    Electronic supplementary material  The online version of this article (doi:10.1186/s13041-015-0148-4) contains supplementary material, which is available to authorized users.

Regulation of STEP61 and tyrosine-phosphorylation of NMDA and AMPA receptors during homeostatic synaptic plasticity