Our biochemical and Diperodon proteomic analysis of the proteins Ginsenoside-F4 associated with the C-terminus of SERT identified vimentin, an intermediate filament in between many other platelet proteins. Based on our 
studies detailed here, we propose that phosphate modification of the SITPETsequence of SERT one at a time exposes the C-terminus domain of SERT for vimentin association. Conversely, following 5HT stimulation, the association between vimentin-SERT is enhanced specifically on the plasma membrane which controls the cellular distribution of SERT on an altered vimentin network. Densitometric scanning of W/B was done on VersaDoc digital imaging system. On each gel, samples were compared with the biotinylation procedure applied to the same amount of cells as determined by the BCA protein assay. The experiments were performed within the linear range of densitometry reading of the SERT band as a function of the amount of protein applied according to control experiments with varying amounts of protein load per lane. Densitometry data were captured as total signal in the rectangular area encompassing the band of study corrected for background; the same rectangular area was used for estimates of the same band in other lanes of gel. Results from different scans were uniform. To determine the involvement of phosphovimentin in the density of SERT on platelet plasma membrane, platelets in PRP were first pretreated with 5HT for 30 min at RT, then the pelleted platelets was biotinylated with membrane impermeable NHS-SS-biotin. Biotinylated platelet plasma membrane proteins were retrieved on streptavidin beads and eluted from the beads. Half of each biotinylated sample was subjected to immunoblot analysis using anti-SERT Ab. The biphasic effect of plasma 5HT on the density of SERT on platelet plasma membrane was observed, as seen previously in hypertension model systems. An intermediate level 5HT-stimulation increased the density of SERT on the platelet; however, at high level, 5HT-stimulation lowered the surface density of SERT compared to untreated platelets. Here, our data demonstrate that the association between SERT and vimentin is altered in a 5HT-dependent manner. Therefore, here we tested whether the cellular distribution of SERT is altered by 5HT-dependent phosphorylation of vimentin. The level of phosphovimentin on the plasma membrane 5HT-stimulated platelet was evaluated.