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Fig. 6 | BMC Biology

Fig. 6

From: Neuronal surface P antigen (NSPA) modulates postsynaptic NMDAR stability through ubiquitination of tyrosine phosphatase PTPMEG

Fig. 6

PTPMEG levels are increased due to less ubiquitination in hippocampal fractions of NSPA-KO mice. a STEP61 tyrosine phosphatase levels and b STEP61 ubiquitination analysis show no differences in hippocampal P2 fractions from WT and NSPA-KO mice. MG-132 treatment equally increased STEP61 levels in WT and NSPA-KO mice (mean ± SEM; n = 4; *P < 0.05; n.s, non-statistical differences, t-test). c Fyn kinase immunoblot show similar band intensities in WT and NSPA-KO mice (mean ± SEM; n = 3; n.s, non-statistical differences in t-test). d The levels of PTPMEG are increased in NSPA-KO compared with WT hippocampal P2 fractions prepared with DMSO (vehicle), which instead become similar under MG-132 treatment (mean ± SEM; n = 3; **P < 0.01, one-way ANOVA, followed Bonferroni’s post hoc test). e NSPA-dependent ubiquitination of PTPMEG. Immunoprecipitated PTPMEG from hippocampal P2 fractions followed by immunoblot with anti-PTPMEG or anti-ubiquitin (P4D1) show ubiquitinated PTPMEG only in WT and not in NSPA-KO or NSPA-TR mice (n = 3). f GluN2A and GluN2B subunits co-immunoprecipitated with PTPMEG, as shown by immunoprecipitation with anti-PTPMEG or control IgG from WT P2 fractions followed by immunoblot with anti-GluN2A and anti-GluN2B antibodies. Source data values are included in Additional file 2

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