Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, USA.
Autophagy. 2022 Oct;18(10):2267-2269. doi: 10.1080/15548627.2022.2100678. Epub 2022 Jul 19.
The conjugation of Atg8-family proteins with phospholipids on the double-membrane phagophore is one of the hallmarks of macroautopahgy/autophagy. However, in the past decades, Atg8-family proteins have also been identified on single-membrane structures, including the phagosome, endosome and lysosome. While the physiological importance of the non-canonical Atg8-family protein conjugation has been demonstrated, the mechanism of this process and the underlying regulation are still not very clear. In a recent paper, Hooper et al. found that during LC3-associated phagocytosis, reactive oxygen species are required for V-ATPase assembly, which is essential for the subsequent LC3 conjugation to the phagosome. Enhanced V-ATPase assembly and the direct engagement of ATG16L1 are also observed in a wide range of non-canonical Atg8-family protein conjugation processes, defining the V-ATPase and ATG16L1 as taking part in a common mechanism.
Atg8 家族蛋白与双层吞噬体磷脂的共轭是巨自噬/自噬的标志之一。然而,在过去的几十年中,Atg8 家族蛋白也被发现在单膜结构上,包括吞噬体、内体和溶酶体。虽然已经证明了非典型 Atg8 家族蛋白共轭的生理重要性,但该过程的机制和潜在调节仍不是很清楚。在最近的一篇论文中,Hooper 等人发现,在 LC3 相关的吞噬作用过程中,活性氧物质对于 V-ATPase 组装是必需的,这对于随后 LC3 与吞噬体的共轭至关重要。增强的 V-ATPase 组装和 ATG16L1 的直接参与也在广泛的非典型 Atg8 家族蛋白共轭过程中观察到,这将 V-ATPase 和 ATG16L1 定义为参与一个共同的机制。