Wan Hong, Lin Kuang, Tsang Siu Man, Uttagomol Jutamas
Queen Mary University of London, Barts and The London School of Medicine and Dentistry, Centre for Clinical and Diagnostic Oral Sciences, Institute of Dentistry, London.
Institute of Psychiatry, King׳s College London, London.
Data Brief. 2015 Dec 3;6:124-34. doi: 10.1016/j.dib.2015.11.049. eCollection 2016 Mar.
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.
本数据文章包含与题为《桥粒芯糖蛋白3通过与E-钙黏蛋白相互作用与Src激活相关》（曾等，2010年）[1]的研究文章相关的扩展补充分析，以及与题为《桥粒芯糖蛋白3：在癌症进展中是助力还是阻碍？》（布朗等，2014年）[2]的综述文章相关的图表。我们在此表明，Src和小窝蛋白-1（Cav-1）在非离子去污剂可溶池中与桥粒芯糖蛋白3（Dsg3）相关联，并且Dsg3水平的调节会反向改变Cav-1复合物中Src的表达。此外，免疫荧光分析显示，与对照细胞相比，过表达Dsg3的细胞中Cav-1/总Src的共定位减少。作为支持，序列分析已在人Dsg3的羧基末端确定了一个区域，该区域有可能与Cav-1的支架结构域结合，Cav-1的支架结构域是已知的Src在Cav-1中的结合位点，并且该区域在18个物种中的大多数以及桥粒芯糖蛋白家族成员中高度保守。基于这些发现，我们提出了一个工作模型，即Dsg3通过与其无活性形式竞争结合Cav-1来激活Src，从而导致Src释放并随后自我激活。
