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首页> 外文期刊>Molecular biology of the cell >An Atg4B Mutant Hampers the Lipidation of LC3 Paralogues and Causes Defects in Autophagosome Closure
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An Atg4B Mutant Hampers the Lipidation of LC3 Paralogues and Causes Defects in Autophagosome Closure

机译：Atg4B突变体阻碍LC3旁系同源物的脂化并导致自噬封闭的缺陷。

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摘要

In the process of autophagy, a ubiquitin-like molecule, LC3/Atg8, is conjugated to phosphatidylethanolamine ( PE) and associates with forming autophagosomes. In mammalian cells, the existence of multiple Atg8 homologues ( referred to as LC3 paralogues) has hampered genetic analysis of the lipidation of LC3 paralogues. Here, we show that overexpression of an inactive mutant of Atg4B, a protease that processes pro-LC3 paralogues, inhibits autophagic degradation and lipidation of LC3 paralogues. Inhibition was caused by sequestration of free LC3 paralogues in stable complexes with the Atg4B mutant. In mutant overexpressing cells, Atg5- and ULK1-positive intermediate autophagic structures accumulated. The length of these membrane structures was comparable to that in control cells; however, a significant number were not closed. These results show that the lipidation of LC3 paralogues is involved in the completion of autophagosome formation in mammalian cells. This study also provides a powerful tool for a wide variety of studies of autophagy in the future.
机译：在自噬过程中，泛素样分子LC3 / Atg8与磷脂酰乙醇胺（PE）结合并结合形成自噬体。在哺乳动物细胞中，多个Atg8同源物（称为LC3旁系同源物）的存在阻碍了LC3旁系同源物脂化的遗传分析。在这里，我们显示Atg4B（处理pro-LC3旁系同源物的蛋白酶）的无活性突变体的过表达抑制了LC3旁系同源物的自噬降解和脂质化。抑制作用是由与Atg4B突变体稳定的复合物中螯合游离LC3旁系同源物引起的。在突变的过表达细胞中，Atg5和ULK1阳性中间自噬结构积累。这些膜结构的长度与对照细胞相当。但是，有很多没有关闭。这些结果表明，LC3旁系同源物的脂质化与哺乳动物细胞中自噬体形成的完成有关。该研究还为将来的自噬研究提供了强大的工具。

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