Chvatchko Y, Howald I, Riezman H
Cell. 1986 Aug 1;46(3):355-64. doi: 10.1016/0092-8674(86)90656-2.
We have purified biosynthetically labeled alpha-factor secreted from transformed yeast alpha cells. This alpha-factor binds specifically to a cells and is internalized by a time-, temperature-, and energy-dependent process. alpha-factor is internalized in an intact form and then rapidly degraded. Two yeast mutants defective in the accumulation of an endocytotic marker, lucifer yellow CH, in the vacuole have been isolated. end1 accumulates invaginations of the plasma membrane, and end2, an internal membrane-bound organelle. One of these mutants, end1, is defective for internalization of alpha-factor. Both of these mutants are defective in pheromone response.
我们已经纯化了从转化的酵母α细胞中分泌的生物合成标记的α因子。这种α因子特异性结合α细胞并通过时间、温度和能量依赖性过程被内化。α因子以完整形式被内化，然后迅速降解。已经分离出两个在液泡中内吞标记物荧光素黄CH积累方面有缺陷的酵母突变体。end1积累质膜内陷，end2积累一种内膜结合细胞器。这些突变体之一end1在α因子内化方面有缺陷。这两个突变体在信息素反应方面都有缺陷。
