Key Laboratory of Pharmaceutical Biotechnology, Department of Biochemistry, College of Life Sciences and School of Stomatology, Affiliated Stomatological Hospital, Nanjing University, Nanjing, P R China.
Mol Imaging. 2013 Mar-Apr;12(2):111-20.
Fas-associated death domain (FADD) is an adaptor molecule for the death receptor subfamily of the tumor necrosis factor receptor superfamily, but it is also required for cell proliferation. FADD protein has the potential to highly oligomerize. FADD self-aggregates in vitro and transfected FADD in mammalian cells induce apoptosis by forming large, filamentous structures termed death effector filaments independent of receptor cross-linking at the plasma membrane. We used fluorescence spectroscopy and three-channel fluorescence resonance energy transfer (FRET) microscopy to qualitatively and quantitatively analyze self-association of FADD and its variants in living cells. Our results demonstrate that FADD self-association not only is determined by its N-terminal death effector domain (h-FADD 1-79) but is also obviously regulated by its C-terminal phosphorylatable tail (h-FADD 183-208).
Fas 相关死亡结构域（FADD）是肿瘤坏死因子受体超家族死亡受体亚家族的衔接分子，但它也是细胞增殖所必需的。FADD 蛋白具有高度寡聚化的潜力。FADD 在体外自聚集，转染的 FADD 在哺乳动物细胞中通过形成称为死亡效应丝的大的、丝状结构诱导凋亡，而无需在质膜上进行受体交联。我们使用荧光光谱和三通道荧光共振能量转移（FRET）显微镜来定性和定量分析活细胞中 FADD 及其变体的自组装。我们的结果表明，FADD 自组装不仅取决于其 N 端死亡效应结构域（h-FADD 1-79），而且还明显受到其 C 端可磷酸化尾（h-FADD 183-208）的调节。
