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. Author manuscript; available in PMC: 2013 Mar 7.
Published in final edited form as: Neuron. 2012 Mar 8;73(5):962–977. doi: 10.1016/j.neuron.2011.12.033

Figure 5. Repeated stress increases the ubiquitination level of GluR1 and NR1 subunits.

Figure 5

(A, B) Representative blots (A) and quantification (B) showing the ubiquitination of GluR1 and NR1 subunits in control vs. stressed (7-day restraint) animals without or with RU486 injection (10 mg/kg). *: p<0.01, t test. Lysates of PFC slices were immunoprecipitated with an antibody against GluR1 or NR1, and then blotted with a ubiquitin antibody. Also shown are the input control, the immunoprecipitation control, and the immunoblots of total proteins in control vs. stressed animals. Note, in stressed rats, the immunoprecipitated GluR1 or NR1 showed ubiquitin staining at a molecular mass heavier than the unmodified protein itself. The ladder of ubiquitinated GluR1 or NR1 is typical of proteins that are polyubiquitinated to signal their degradation. (C) Ubiquitination of GluR2, NR2A, NR2B, SAP97 and PSD-95 in control vs. stressed (7-day restraint) animals.