Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast
Apg10p, a novel protein-conjugating enzyme essential for autophagy in yeast
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DOI：
10.1093/emboj/18.19.5234
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发表时间：
1999-10-01
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：
Shintani, T;Mizushima, N;Ohsumi, Y
自噬是细胞质成分大量降解的细胞过程。Apg12p是一种与泛素没有明显相似性的修饰剂，它附着在Apg5p上对酵母的自噬至关重要。该反应以泛素化样方式进行，需要Apg7p和Apg10p， Apg7p与泛素激活酶（E1）有相当的相似性，并且发现Apg7p通过ATP水解激活Apg12p。另一方面，Apg10p与其他已知功能的蛋白质没有明显的相似性。本研究表明，Apg10p被Apg7p激活后，Apg12p转移到Apg10p的Cys-133残基上，形成Apg12p-Apg10p硫酯，表达Apg10p（C133S）的细胞不会产生Apg12p- apg5p偶联物，导致细胞自噬和氨基肽酶i的胞质-液泡靶向缺陷。这些发现表明，Apg10p是一种新型的蛋白质偶联酶，在Apg12p- apg5d偶联途径中起作用。
Autophagy is a cellular process for bulk degradation of cytoplasmic components. The attachment of Apg12p, a modifier with no significant similarity to ubiquitin, to Apg5p is crucial for autophagy in yeast, This reaction proceeds in a ubiquitination-like manner, and requires Apg7p and Apg10p, Apg7p exhibits a considerable similarity to ubiquitin-activating enzyme (E1) and is found to activate Apg12p with ATP hydrolysis. Apg10p, on the other hand, shows no significant similarity to other proteins whose functions are known. Here, we show that after activation by Apg7p, Apg12p is transferred to the Cys-133 residue of Apg10p to form an Apg12p-Apg10p thioester, Cells expressing Apg10p(C133S) do not generate the Apg12p-Apg5p conjugate, which leads to defects in autophagy and cytoplasm-to-vacuole targeting of aminopeptidase I. These findings indicate that Apg10p is a new type of protein-conjugating enzyme that functions in the Apg12p-Apg5D conjugation pathway.