Fig. 5: Ischemic stroke alters protein phosphorylation at the PSD. | Communications Biology

Fig. 5: Ischemic stroke alters protein phosphorylation at the PSD.

From: Post-ischemic ubiquitination at the postsynaptic density reversibly influences the activity of ischemia-relevant kinases

Fig. 5

a The same homogenates used for ubiquitination studies were subjected to phospho-proteome analysis. The Volcano plot shows a significant increase and decrease of phosphorylation of 66 and 8 phospho-peptides, respectively, when comparing ipsilateral to control samples. Data were pooled from 2 to 3 MS experiments. Significance at fold change = 2 with P < 0.05 (two-tailed unpaired t-test). b Heatmap depicting hierarchical clustering of identified phospho-peptide abundances in control and ipsilateral samples. c GO analysis showing enrichment of proteins with changed post-ischemic phosphorylation at the PSD. Asterisks indicate terms with the most significant enrichment. d Cytosolic, synaptic membrane, and PSD-enriched fractions were obtained from ipsilateral cortices after MCAO/1 h reperfusion and stained for phospho-tyrosine. n = 7 animals/group; *P < 0.0001 from C and M; one-way ANOVA with Bonferroni test. e Cortical detergent-insoluble lysates from sham and MCAO-treated (ipsilateral and contralateral) animals were probed for the presence of phospho-tyrosine. n = 5 animals/group; *P < 0.0001 from s and c; one-way ANOVA with Bonferroni test. f Same as in e, but probed for phospho-serine/threonine. n = 5 animals/group. c contralateral, C cytosol, GO gene ontology, i ipsilateral, M membrane, P postsynaptic density, S serine, s sham, T threonine, Y tyrosine. Data are expressed as mean ± s.e.m.

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