Pathological Role of Peptidyl-Prolyl Isomerase Pin1 in the Disruption of Synaptic Plasticity in Alzheimer’s Disease

Figure 4

Blocking of Pin1 activity increases the modification of ubiquitin in PSD proteins. C57/BL6 cortical neurons at 21 DIV were incubated with PiB and MG-132 for 24 h and transfected by Pin1 shRNA or control shRNA lentivirus for 48 h, respectively; the PSDs were isolated and analyzed with Western blot. (a) Coimmunoprecipitation between Pin1 and Shank3 proteins. (b) Total Pin1 proteins were knocked down ( dishes for each experimental condition, ; ). (c) Ladders of Shank3 proteins after the loss of Pin1 activity. (d) Ubiquitinated Shank3 proteins were enriched by ubiquitin-affinity purification and recognized by Shank3 antibody in Western blot.

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