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. Author manuscript; available in PMC: 2016 Nov 4.
Published in final edited form as: Neuron. 2015 Oct 22;88(3):528–538. doi: 10.1016/j.neuron.2015.09.037

Figure 5.

Figure 5

Anchoring of monoamine receptors is crucial for the transformation of transient LTP/D eligibility traces.

(A) The β2AR-specific antagonist ICI 118,551 (1 μM) prevents the transformation of the LTP eligibility trace by NE (95.2 ± 5.3%). The magenta line depicts control LTP (data from Fig1D).

(B) The 5-HT2CR specific antagonist RS 102221 (1 μM) prevents the transformation of the LTD eligibility trace by 5-HT (99.8 ± 8.2%). The blue line depicts control LTD (data from Fig1E). (C) β2AR directly interacts with PSD-95, and its c-terminal peptide DSPL disrupts this interaction.

(D) DSPL, but not the scrambled peptide DAPA, abolished the NE-mediated transformation of the LTP eligibility trace (DSPL: 96.1 ± 8.2%; DAPA: 127.8 ± 7.9%).

(E) The C-terminal peptide 2C-ct prevents the interaction between 5-HT2CR and PDZ-containing proteins such as PSD-95.

(F) 2C-ct, but not the control peptide CSSA, blocked transformation of the LTD eligibility trace by 5-HT (2C-ct: 102.9 ± 3.7%; CSSA: 82.6 ± 3.9%).

See also Fig S3-4.