Suzuki Kuninori, Kubota Yuka, Sekito Takayuki, Ohsumi Yoshinori
Department of Cell Biology, Division of Molecular Cell Biology, National Institute for Basic Biology, Nishigonaka 38, Okazaki, 444-8585 Japan.
Genes Cells. 2007 Feb;12(2):209-18. doi: 10.1111/j.1365-2443.2007.01050.x.
Autophagy is a bulk degradation process that is conserved in eukaryotic cells and functions in the turnover of cytoplasmic materials and organelles. When eukaryotic cells face nutrient starvation, the autophagosome, a double-membraned organelle, is generated from the pre-autophagosomal structure (PAS). In the yeast Saccharomyces cerevisiae, 16 ATG (autophagy-related) genes are essential for autophagosome formation. Most of the Atg proteins are involved in the PAS, leading to autophagosome production. However, the mechanism of PAS organization remains to be elucidated. Here, we performed a systematic and quantitative analysis by fluorescence microscopy to develop a hierarchy map of Atg proteins involved in PAS organization. This analysis suggests that Atg17p is the most basic protein in PAS organization: when it is specifically targeted to the plasma membrane, other Atg proteins are recruited to that location, suggesting that Atg17p acts as a scaffold protein to organize Atg proteins to the PAS.
自噬是一种在真核细胞中保守的大量降解过程,在细胞质物质和细胞器的周转中发挥作用。当真核细胞面临营养饥饿时,自噬体(一种双膜细胞器)由自噬前体结构(PAS)产生。在酿酒酵母中,16个ATG(自噬相关)基因对自噬体形成至关重要。大多数Atg蛋白参与PAS,导致自噬体产生。然而,PAS组织的机制仍有待阐明。在这里,我们通过荧光显微镜进行了系统和定量分析,以绘制参与PAS组织的Atg蛋白的层次图。该分析表明,Atg17p是PAS组织中最基本的蛋白质:当它特异性定位于质膜时,其他Atg蛋白会被招募到该位置,这表明Atg17p作为一种支架蛋白将Atg蛋白组织到PAS中。