哺乳动物 ATG12-ATG5-ATG16L1 复合物在自噬和相关过程中的功能。
Toward the function of mammalian ATG12-ATG5-ATG16L1 complex in autophagy and related processes.
机构信息
a Department of Molecular Medicine, Institute of Basic Medical Sciences and Centre for Cancer Cell Reprogramming , University of Oslo , Oslo , Norway .
b Department of Medical Biochemistry and Biophysics , University of Umeå , Umeå , Sweden .
出版信息
Autophagy. 2019 Aug;15(8):1485-1486. doi: 10.1080/15548627.2019.1618100. Epub 2019 May 23.
The machinery that decorates autophagic membranes with lipid-conjugated LC3/GABARAP is not yet fully understood. We recently reported the purification of the full-length ATG12-ATG5-ATG16L1 complex, and in reconstitution experiments with purified ATG7, ATG3, and LC3/GABARAP in vitro, together with rescue experiments in knockout cells, important aspects of the complete lipidation reaction were revealed. Hitherto unobserved membrane-binding regions in ATG16L1 were found, contributing to properties that explain the crucial role of this protein in membrane targeting and LC3/GABARAP lipidation in macroautophagy/autophagy and other related processes.
目前，人们对于将脂类连接的 LC3/GABARAP 缀合到自噬膜上的机制还不是完全了解。我们最近报道了全长 ATG12-ATG5-ATG16L1 复合物的纯化，并在体外与纯化的 ATG7、ATG3 和 LC3/GABARAP 进行了重构实验，以及在敲除细胞中的拯救实验，揭示了完整脂化反应的重要方面。在 ATG16L1 中发现了迄今为止尚未观察到的膜结合区域，这些区域有助于解释该蛋白在膜靶向和 LC3/GABARAP 脂质化中的关键作用，在巨自噬/自噬和其他相关过程中也是如此。
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