Evidence for Dsg3 in regulating Src signaling by competing with it for binding to caveolin-1

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• 作者：Hong Wan^a ; ^{h.wan@qmul.ac.uk" class="auth_mail" title="E-mail the corresponding author} ; Kuang Lin^b ; Siu Man Tsang^a ; Jutamas Uttagomol^a
• 关键词：Desmoglein ; Src signaling ; Caveolin ; Sequence alignment
• 刊名：Data in Brief
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：6
• 期：Complete
• 页码：124-134
• 全文大小：4008 K

文摘

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">[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.