Jung Joanna, Wang Jessica, Groenendyk Jody, Lee Dukgyu, Michalak Marek, Agellon Luis B
Departments of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
School of Human Nutrition, McGill University, Ste. Anne de Bellevue, Quebec, H9X 3V9, Canada.
Biochem Biophys Res Commun. 2017 Nov 4;493(1):202-206. doi: 10.1016/j.bbrc.2017.09.046. Epub 2017 Sep 11.
Calnexin is a type 1 integral endoplasmic reticulum membrane molecular chaperone with an endoplasmic reticulum luminal chaperone domain and a highly conserved C-terminal domain oriented to the cytoplasm. Fabp5 is a cytoplasmic protein that binds long-chain fatty acids and other lipophilic ligands. Using a yeast two-hybrid screen, immunoprecipitation, microscale thermophoresis analysis and cellular fractionation, we discovered that Fabp5 interacts with the calnexin cytoplasmic C-tail domain at the endoplasmic reticulum. These observations identify Fabp5 as a previously unrecognized calnexin binding partner.
钙连接蛋白是一种1型内质网整合膜分子伴侣，具有内质网腔伴侣结构域和一个面向细胞质的高度保守的C末端结构域。脂肪酸结合蛋白5（Fabp5）是一种结合长链脂肪酸和其他亲脂性配体的细胞质蛋白。通过酵母双杂交筛选、免疫沉淀、微量热泳分析和细胞分级分离，我们发现Fabp5在内质网处与钙连接蛋白的细胞质C末端结构域相互作用。这些观察结果表明Fabp5是一种先前未被识别的钙连接蛋白结合伴侣。
