钙调蛋白的N端和C端结构域介导FADD与TRADD的相互作用。
N-terminal and C-terminal domains of calmodulin mediate FADD and TRADD interaction.
作者信息
Papoff Giuliana, Trivieri Nadia, Marsilio Sonia, Crielesi Roberta, Lalli Cristiana, Castellani Loriana, Balog Edward M, Ruberti Giovina
机构信息
National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy.
National Research Council, Institute of Cell Biology and Neurobiology, Campus Adriano Buzzati-Traverso, Monterotondo, Rome, Italy; Department of Human Sciences, Society and Health, University of Cassino, Cassino, Italy.
出版信息
PLoS One. 2015 Feb 2;10(2):e0116251. doi: 10.1371/journal.pone.0116251. eCollection 2015.
FADD (Fas-associated death domain) and TRADD (Tumor Necrosis Factor Receptor 1-associated death domain) proteins are important regulators of cell fate in mammalian cells. They are both involved in death receptors mediated signaling pathways and have been linked to the Toll-like receptor family and innate immunity. Here we identify and characterize by database search analysis, mutagenesis and calmodulin (CaM) pull-down assays a calcium-dependent CaM binding site in the α-helices 1-2 of TRADD death domain. We also show that oxidation of CaM methionines drastically reduces CaM affinity for FADD and TRADD suggesting that oxidation might regulate CaM-FADD and CaM-TRADD interactions. Finally, using Met-to-Leu CaM mutants and binding assays we show that both the N- and C-terminal domains of CaM are important for binding.
FADD（Fas相关死亡结构域）和TRADD（肿瘤坏死因子受体1相关死亡结构域）蛋白是哺乳动物细胞中细胞命运的重要调节因子。它们都参与死亡受体介导的信号通路，并与Toll样受体家族和先天免疫相关。在这里，我们通过数据库搜索分析、诱变和钙调蛋白（CaM）下拉实验，在TRADD死亡结构域的α螺旋1-2中鉴定并表征了一个钙依赖性CaM结合位点。我们还表明，CaM甲硫氨酸的氧化会大幅降低CaM对FADD和TRADD的亲和力，这表明氧化可能调节CaM-FADD和CaM-TRADD的相互作用。最后，使用甲硫氨酸到亮氨酸的CaM突变体和结合实验，我们表明CaM的N端和C端结构域对结合都很重要。
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