Atg8 regulates vacuolar membrane dynamics in a lipidation-independent manner in Pichia pastoris
Atg8 regulates vacuolar membrane dynamics in a lipidation-independent manner in Pichia pastoris
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DOI：
10.1242/jcs.070045
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发表时间：
2010-12-01
影响因子：
4
通讯作者：
Sakai, Yasuyoshi
中科院分区：
文献类型：
--
作者：
Tamura, Naoki;Oku, Masahide;Sakai, Yasuyoshi
Atg 8是一种泛素样蛋白，沿着其脂化系统，在所有真核细胞中自噬都是必需的。Atg 8的脂化形式在自噬期间锚定在自噬体膜上。在这里，我们证明了一个以前未知的作用Atg 8在液泡膜动力学。在甲醇营养型毕赤酵母中，空泡被发现融合成为一个单一的球形空泡过程中，从葡萄糖到甲醇的培养基中的适应。Atg 8负责巴斯德毕赤酵母在甲醇适应过程中的液泡融合。虽然液泡融合需要在C-末端加工Atg 8，但它不需要Atg 8的脂化进行自噬。这是第一次报告的功能，任何Atg 8蛋白家族成员的过程中，而不是自噬是独立的脂化。
Atg8 is a ubiquitin-like protein that is required, along with its lipidation system, for autophagy in all eukaryotic cells. The lipidated form of Atg8 is anchored on the autophagosomal membrane during autophagy. Here, we demonstrate a previously unknown role for Atg8 in vacuolar membrane dynamics. In the methylotrophic yeast Pichia pastoris, vacuoles were found to fuse to become a single spherical vacuole during adaptation from glucose-to methanol-containing medium. Atg8 is responsible for the vacuolar fusion in P. pastoris during this adaptation to methanol. Although vacuole fusion required processing of Atg8 at the C-terminus, it did not require lipidation of Atg8 for autophagy. This is the first report of the function of any Atg8 protein family member in a process other than autophagy that is independent of lipidation.