The anti-N-methyl-D-aspartate receptor (NMDAR) encephalitis is an autoimmune disorder characterized by specific autoantibodies targeting the GluN1 subunit of postsynaptic NMDARs. Here, we investigated the effects of patient monoclonal anti-GluN1 antibodies on the synaptic signalling and plasticity molecules CaMKII and DAPK1 and their related pathways.We incubated primary hippocampal cell cultures (div 14-21) with patient-derived monoclonal anti-GluN1 or control antibodies. Thereafter, we induced chemical LTP and/or treated cells with the DAPK1 inhibitor TC-DAPK6. We then analysed NMDARs GluN1 and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPAR) GluA1 synaptic density using direct stochastic reconstruction microscopy (dSTORM). Furthermore, we investigated CaMKII localization, using structured illumination microscopy (SIM) as well as activation, using confocal laser scanning microscopy (cLSM), paired with spectral unmixing. We additionally performed proteomic analysis to get deeper insight on the antibodies effects on CaMKII and DAPK1 pathways.We successfully established stable LTP induction and staining for GluN1, GluA1, CaMKII and postsynaptic markers, for both dSTORM and SIM. We established TC-DAPK6 treatment to inhibit co-localisation of DAPK1 within synapses. Additionally we succeeded in transfecting neurons to perform cLSM with specialized CaMKII constructs, carrying different fluorescence proteins. Furthermore, we investigated the combined application of LTP, human GluN1 antibodies, and/or TC-DAPK6 on localisation and/or activation of NMDAR, AMPAR and CaMKII. With this, we can provide evidence for antibody-induced, CaMKII dependent remodelling of synapses, which may be relevant for disturbed synaptic plasticity in NMDAR encephalitis