Lisanti M P, Caras I W, Rodriguez-Boulan E
Department of Cell Biology and Anatomy, Cornell University Medical College, New York, NY 10021.
J Cell Sci. 1991 Jul;99 ( Pt 3):637-40. doi: 10.1242/jcs.99.3.637.
We have shown that addition of the C-terminal 37 amino acids of decay-accelerating factor (DAF) to secretory proteins leads to glycosyl-phosphatidyl-inositol (GPI) anchoring and apical surface expression in MDCK cells. Theoretically, transferred apical sorting information may reside in the glycolipid-anchor moiety or the DAF sequence (9 amino acids) that remains after signal cleavage and GPI attachment. We show here that removal of eight of these nine remaining amino acids, thereby creating a minimal GPI-attachment signal, results in apical expression of GPI-anchored human growth hormone. These data argue that the apical sorting information conveyed by the C terminus of DAF is related to its ability to direct GPI attachment, rather than to a specific sequence that remains in the fusion protein.
我们已经证明，将衰变加速因子（DAF）的C末端37个氨基酸添加到分泌蛋白中，会导致糖基磷脂酰肌醇（GPI）锚定以及在MDCK细胞中的顶端表面表达。理论上，转移的顶端分选信息可能存在于糖脂锚定部分或信号切割和GPI附着后剩余的DAF序列（9个氨基酸）中。我们在此表明，去除这9个剩余氨基酸中的8个，从而产生一个最小的GPI附着信号，会导致GPI锚定的人生长激素的顶端表达。这些数据表明，DAF的C末端传达的顶端分选信息与其指导GPI附着的能力有关，而不是与融合蛋白中保留的特定序列有关。
