Abstract
This data article contains extended, complementary analysis related to the research articles entitled “Desmoglein 3, via an interaction with E-cadherin, is associated with activation of Src” (Tsang et al., 2010) [1] and figures related to the review article entitled “Desmoglein 3: a help or a hindrance in cancer progression?” (Brown et al., 2014) [2]. We show here that both Src and caveolin-1 (Cav-1) associate with Dsg3 in a non-ionic detergent soluble pool and that modulation of Dsg3 levels inversely alters the expression of Src in the Cav-1 complex. Furthermore, immunofluorescence analysis revealed a reduced colocalization of Cav-1/total Src in cells with overexpression of Dsg3 compared to control cells. In support, the sequence analysis has identified a region within the carboxyl-terminus of human Dsg3 for a likelihood of binding to the scaffolding domain of Cav-1, the known Src binding site in Cav-1, and this region is highly conserved across most of 18 species as well as within desmoglein family members. Based on these findings, we propose a working model that Dsg3 activates Src through competing with its inactive form for binding to Cav-1, thus leading to release of Src followed by its auto-activation.
Highlights
This data article contains extended, complementary analysis related to the research articles entitled “Desmoglein 3, via an interaction with E-cadherin, is associated with activation of Src” (Tsang et al, 2010) [1] and figures related to the review article entitled “Desmoglein 3: a help or a hindrance in cancer progression?” (Brown et al, 2014) [2]
We show here that both Src and caveolin-1 (Cav-1) associate with Desmoglein 3 (Dsg3) in a non-ionic detergent soluble pool and that modulation of Dsg3 levels inversely alters the expression of Src in the Cav-1 complex
Image, sequence alignment, graph Confocal microscope, co-immunoprecipitation, proximity ligation assay, bioinformatics filtered, analyzed Cell culture, RNAi mediated knockdown of Dsg3, calcium depletion and repletion in vitro analyses of protein-protein interaction and protein sequence alignment Original source of protein sequences used for alignment is from the NCBI Proteins Data is with this article
Summary
Image, sequence alignment, graph Confocal microscope, co-immunoprecipitation, proximity ligation assay, bioinformatics filtered, analyzed Cell culture, RNAi mediated knockdown of Dsg, calcium depletion and repletion in vitro analyses of protein-protein interaction and protein sequence alignment Original source of protein sequences used for alignment is from the NCBI Proteins Data is with this article. The protein sequence analysis identifies a putative region for binding the caviolin-1 scaffolding domain enriched in aromatic amino acids [10] in Dsg which is highly conserved across most of 18 species (Fig. 3) as well as within the Dsg family members (Fig. 4) This potential binding site is located within the ICS domain of C-terminus of Dsg at 788-798aa, an 11aa stretch which contains 4 aromatic aa residues and which likely competes with the inactive Src for binding to the scaffolding domain in caveolin-1 [10]. This working model opens up a new avenue for future research
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