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Fig. 2. Two-dimensional analysis of the proteins interacting with the C-termini of mouse 5-HT₄R splice variants. Proteins that bind to the C-terminus of the 5-HT_4(a)R and 5-HT_4(e)R variants were purified by affinity chromatography, separated by 2D electrophoresis and stained with silver. (A) 2D gels obtained with the C-t(a)wt and the C-t(e)wt peptides are illustrated. Arrows indicate the position of spots or trains of spots that were specifically retained by the C-t(a)wt and the C-t(b)wt peptides but not truncated peptides lacking their PDZ ligand [C-t(a)SCF and C-t(e)PVPV, respectively]. (B,C) Proteins recruited by affinity chromatography using the C-t(a)wt, C-t(b)wt, C-t(e)wt, C-t(a)SCF or C-t(e)PVPV peptides were separated by 2D electrophoresis and stained with silver. (B, top) Areas of interest of 2D gels showing the specific recruitment of ten spots by the 5-HT_4(a)R C-terminus [C-t(a)wt peptide] via a PDZ-based mechanism. (C, top) Areas of interest of 2D gels showing the specific recruitment of three spots by the 5-HT_4(e)R C-terminus [C-t(e)wt peptide] via a PDZ-based mechanism. The data are representative of four experiments performed independently.

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