Ca2+ 是控制 Snf1 介导的 Atg1 激活的重要信号分子。

Autophagy Pub Date : 2024-11-01 Epub Date: 2024-08-11 DOI:10.1080/15548627.2024.2389483
Yanyang Wu, Cong Yi
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引用次数: 0

摘要

大自噬/自噬对维持葡萄糖稳态至关重要,但细胞感知葡萄糖饥饿并启动自噬的机制尚未完全清楚。最近,我们报道了Ca2+触发的Snf1-Bmh1/Bmh2-Atg11复合物的组装在葡萄糖饥饿时启动了自噬。我们的研究发现,在葡萄糖饥饿过程中,液泡 Ca2+ 的外流会增加细胞质 Ca2+ 水平,从而激活蛋白激酶 Rck2。Rck2 介导的 Atg11 磷酸化增强了它与 Bmh1 和 Bmh2 的相互作用。这种相互作用将位于液泡膜上的 Snf1-Sip1-Snf4 复合物招募到吞噬体组装位点(PAS),从而激活 Atg1 并启动自噬。总之,我们发现了一种以前未曾认识到的参与葡萄糖饥饿诱导自噬的信号通路,其中 Ca2+ 作为一种基本信号分子,将能量胁迫与自噬启动复合物的形成联系起来。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Ca2+ as an essential signaling molecule controlling Snf1-mediated Atg1 activation.

Macroautophagy/autophagy is essential for maintaining glucose homeostasis, but the mechanisms by which cells sense glucose starvation and initiate autophagy are not yet fully understood. Recently, we reported that the assembly of a Ca2+-triggered Snf1-Bmh1/Bmh2-Atg11 complex initiates autophagy in response to glucose starvation. Our research reveals that during glucose starvation, the efflux of vacuolar Ca2+ increases cytoplasmic Ca2+ levels, which activates the protein kinase Rck2. Rck2-mediated phosphorylation of Atg11 enhances its interaction with Bmh1 and Bmh2. This interaction recruits the Snf1-Sip1-Snf4 complex, which is located on the vacuolar membrane, to the phagophore assembly site (PAS), leading to the activation of Atg1 and the initiation of autophagy. In summary, we have identified a previously unrecognized signaling pathway involved in glucose starvation-induced autophagy, where Ca2+ acts as a fundamental signaling molecule that links energy stress to the formation of the autophagy initiation complex.Abbreviation: AMPK: AMP-activated protein kinase; ATG: autophagy related; co-IP: co-immunoprecipitation; MAPK: mitogen-activated protein kinase; PAS: phagophore assembly site; ULK1: unc-51 like autophagy activating kinase 1.

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