Li Ziyang, Mochida Keisuke, Nakatogawa Hitoshi
Cell Biology Center, Institute of Integrated Research, Institute of Science Tokyo, Yokohama, Japan.
School of Life Science and Technology, Institute of Science Tokyo, Yokohama, Japan.
Nat Commun. 2024 Dec 17;15(1):10670. doi: 10.1038/s41467-024-55045-9.
Lysosome/vacuole-mediated intracellular degradation pathways, collectively known as autophagy, play crucial roles in the maintenance and regulation of various cellular functions. However, little is known about the relationship between different modes of autophagy. In the budding yeast Saccharomyces cerevisiae, nitrogen starvation triggers both macronucleophagy and micronucleophagy, in which nuclear components are degraded via macroautophagy and microautophagy, respectively. We previously revealed that Atg39-mediated macronucleophagy is important for cell survival under nitrogen starvation; however, the underlying mechanism remains unknown. Here, we reveal that defective Atg39-mediated macronucleophagy leads to the hyperactivation of micronucleophagy, resulting in the excessive transport of various nuclear components into the vacuole. Micronucleophagy occurs at the nucleus-vacuole junction (NVJ). We show that nuclear membrane proteins localized to the NVJ, including Nvj1, which is responsible for micronucleophagy, are degraded via macronucleophagy. Therefore, defective Atg39-mediated macronucleophagy results in the accumulation of Nvj1, which contributes to micronucleophagy enhancement. Blocking micronucleophagy almost completely suppresses cell death caused by the absence of Atg39, whereas enhanced micronucleophagy correlates with death in Atg39-mutant cells under nitrogen starvation. These results suggest that macronucleophagy modulates micronucleophagy in order to prevent the excess removal of nuclear components, thereby maintaining nuclear and cellular homeostasis during nitrogen starvation.
溶酶体/液泡介导的细胞内降解途径统称为自噬,在维持和调节各种细胞功能中发挥着关键作用。然而,关于不同自噬模式之间的关系却知之甚少。在芽殖酵母酿酒酵母中,氮饥饿会触发大核自噬和微核自噬,其中核成分分别通过巨自噬和微自噬进行降解。我们之前揭示了Atg39介导的大核自噬对氮饥饿条件下的细胞存活很重要;然而,其潜在机制仍然未知。在这里,我们揭示了有缺陷的Atg39介导的大核自噬会导致微核自噬的过度激活,从而导致各种核成分过度转运到液泡中。微核自噬发生在核-液泡交界处(NVJ)。我们表明,定位于NVJ的核膜蛋白,包括负责微核自噬的Nvj1,会通过大核自噬被降解。因此,有缺陷的Atg39介导的大核自噬会导致Nvj1的积累,这有助于增强微核自噬。阻断微核自噬几乎完全抑制了因Atg39缺失引起的细胞死亡,而增强的微核自噬与氮饥饿条件下Atg39突变细胞的死亡相关。这些结果表明,大核自噬调节微核自噬,以防止核成分的过度清除,从而在氮饥饿期间维持核和细胞的稳态。