Markham Nicholas O, Cooper Tracy, Goff Matthew, Gribben Erin M, Carnahan Robert H, Reynolds Albert B
Department of Cancer Biology, Vanderbilt University Medical Center, 2220 Pierce Avenue, Nashville, TN 37232, USA.
Hybridoma (Larchmt). 2012 Aug;31(4):246-54. doi: 10.1089/hyb.2012.0009.
The coiled-coil domain-containing delta-interacting protein A (DIPA) is a transcription factor implicated in developmental regulation. DIPA is the first protein discovered to selectively interact with the p120-catenin (p120) isoform 1, an alternatively spliced form of p120 expressed preferentially in mesenchymal cells. Although a small fraction of p120 can be observed in the nucleus under certain circumstances, the vast majority of it associates with classical cadherins at adherens junctions. We observed for the first time that a discrete fraction of DIPA exists at cell-cell junctions, in addition to its predominantly nuclear localization. Thus, the p120-DIPA interaction may regulate cell signaling and/or transcriptional events, as has been described previously for β-catenin and the LEF/TCF transcription factor family. To facilitate further study of DIPA and to determine the physiological relevance of its interaction with p120, we have generated and characterized a panel of five DIPA-specific monoclonal antibodies (MAbs) that function in immunoblotting, immunoprecipitation, and immunofluorescence assays.
含卷曲螺旋结构域的δ相互作用蛋白A（DIPA）是一种参与发育调控的转录因子。DIPA是首个被发现能与p120连环蛋白（p120）亚型1选择性相互作用的蛋白，p120是p120的一种选择性剪接形式，优先在间充质细胞中表达。尽管在某些情况下可在细胞核中观察到一小部分p120，但绝大多数p120在黏附连接处与经典钙黏着蛋白结合。我们首次观察到，除了主要定位于细胞核外，DIPA在细胞间连接处也有离散分布。因此，p120-DIPA相互作用可能如先前针对β-连环蛋白和LEF/TCF转录因子家族所描述的那样，调节细胞信号传导和/或转录事件。为便于进一步研究DIPA并确定其与p120相互作用的生理相关性，我们制备并鉴定了一组五种DIPA特异性单克隆抗体（MAb），它们可用于免疫印迹、免疫沉淀和免疫荧光检测。
