Life Sciences Institute and Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
Cell Res. 2017 Feb;27(2):161-162. doi: 10.1038/cr.2017.4. Epub 2017 Jan 10.
One of the key questions regarding macroautophagy/autophagy is the mechanism through which the transmembrane protein ATG9 functions in delivering membrane to the expanding phagophore, the sequestering compartment that matures into an autophagosome. In a recent study, Zhou et al. identified a novel mechanism that regulates ATG9 trafficking from the plasma membrane and trans-Golgi network, which involves two conserved sorting signals required for ATG9 interaction with the AP1/2 adaptor complex and phosphorylation of ATG9 at Tyr8 by SRC kinase and at Ser14 by ULK1 for proper function during basal and starvation-induced autophagy.
关于巨自噬/自噬的一个关键问题是跨膜蛋白 ATG9 如何在将膜递送至扩大的吞噬体(即成熟为自噬体的隔离区)中发挥作用。在最近的一项研究中,Zhou 等人发现了一种新的机制,该机制调节 ATG9 从质膜和高尔基网络中的运输,该机制涉及两个保守的分选信号,这些信号对于 ATG9 与 AP1/2 衔接复合物的相互作用以及 SRC 激酶对 ATG9 的 Tyr8 残基和 ULK1 对 Ser14 残基的磷酸化是必需的,这些磷酸化对于基础和饥饿诱导的自噬期间的正常功能至关重要。