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. 2021 Sep 7;134(17):jcs257972. doi: 10.1242/jcs.257972

Fig. 3.

Fig. 3.

cLTP- and TTX-induced up scaling treatments increase phosphorylation of GluA1 S845 and reduce binding of β-adaptin to GluA1. (A) Representative immunoblots and quantitative analysis of co-IP of GluA1 with β-adaptin from cultured cortical neurons in the presence or absence of inhibition of dynamin by Dynole (1 µM for 30 min). Mean±s.e.m. of n=3 different cultures. *P<0.05 (unpaired two-tailed Student’s t-test). (B) Representative immunoblots and quantitative analysis of GluA1 S845 phosphorylation (pGluA1-S845) with or without cLTP induction. Mean±s.e.m. of n=7 different cultures. ***P<0.001 (unpaired two-tailed Student's t-test). (C) Representative immunoblots and quantitative analysis of co-IP of GluA1 with β-adaptin from cultured cortical neurons with and without cLTP induction. Mean±s.e.m. of n=4 different cultures. ****P<0.0001 (unpaired two-tailed Student's t-test). (D) Representative immunoblots and quantitative analysis of GluA1 S845 phosphorylation in control neurons, or neurons treated with either TTX or FK506. Mean±s.e.m. of n=15 western blots using samples from 7 different cultures. **P<0.01, ****P<0.0001 (one-way ANOVA with uncorrected Fisher's LSD). (E) Representative immunoblots and quantitative analysis of co-IP of GluA1 from cultured cortical neurons showing that TTX treatment (2 µM for 48 h) and FK506 treatment (5 µM for 48 h) decrease β-adaptin binding to GluA1. Mean±s.e.m. of n=3 different cultures. **P<0.01 (one-way ANOVA with uncorrected Fisher's LSD). GluA1 (A–C,E) and actin (D) are shown as loading controls used for normalization. Molecular mass markers are indicated in kDa.