Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway
Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway
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DOI：
10.1093/emboj/18.14.3888
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发表时间：
1999-07-15
期刊：
影响因子：
11.4
通讯作者：
Ohsumi, Y
中科院分区：
文献类型：
--
作者：
Mizushima, N;Noda, T;Ohsumi, Y
自噬是真核细胞普遍存在的一种细胞内整体降解系统。在这个过程中，细胞质成分被封闭在自噬体中并被递送到溶酶体/空泡。我们最近发现，蛋白质缀合系统，其中Apg 12 p共价连接到Apg 5 p，是必不可少的酵母自噬。在这里，我们描述了一种新的卷曲螺旋蛋白，Apg 16 p，自噬必不可少的。Apg 16 p与Apg 12 p结合的Apg 5 p相互作用，不太优先与未结合的Apg 5 p相互作用。此外，Apg 16 p的卷曲螺旋结构域介导自身多聚化，导致Apg 5 p分子交联并形成稳定的蛋白质复合物。Apg 16 p对于Apg 12 p-Apg 5 p缀合反应不是必需的。这些结果表明，Apg 12 p-Apg 5 p缀合物需要Apg 16 p来完成其在自噬途径中的作用，Apg 16 p是形成Apg 12 p-Apg 5 p-Apg 16 p多聚体的关键分子。
Autophagy is an intracellular bulk degradation system that is ubiquitous for eukaryotic cells. In this process, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. We recently found that a protein conjugation system, in which Apg12p is covalently attached to Apg5p, is indispensable for autophagy in yeast. Here, we describe a novel coiled-coil protein, Apg16p, essential for autophagy. Apg16p interacts with Apg12p-conjugated Apg5p and less preferentially with unconjugated Apg5p, Moreover, the coiled-coil domain of Apg16p mediates self-multimerization that leads to cross-linking of Apg5p molecules and formation of a stable protein complex. Apg16p is not essential for the Apg12p-Apg5p conjugation reaction. These results suggest that the Apg12p-Apg5p conjugate requires Apg16p to accomplish its role in the autophagy pathway, and Apg16p is a key molecule as a linker to form the Apg12p-Apg5p-Apg16p multimer.