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Atg35, a micropexophagy-specific protein that regulates micropexophagic apparatus formation in Pichia pastoris

机译:Atg35,一种微毒素特异性蛋白,可调节巴斯德毕赤酵母中的微毒素装置

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摘要

Autophagy-related (Atg) pathways deliver cytosol and organelles to the vacuole in double-membrane vesicles called autophagosomes, which are formed at the phagophore assembly site (PAS), where most of the core Atg proteins assemble. Atg28 is a component of the core autophagic machinery partially required for all Atg pathways in Pichia pastoris. This coiled-coil protein interacts with Atg17 and is essential for micropexophagy. However, the role of Atg28 in micropexophagy was unknown. We used the yeast two-hybrid system to search for Atg28 interaction partners from P. pastoris and identified a new Atg protein, named Atg35. The atg35Δ mutant was not affected in macropexophagy, cytoplasm-to-vacuole targeting or general autophagy. However, both Atg28 and Atg35 were required for micropexophagy and for the formation of the micropexophagic apparatus (MIPA). This requirement correlated with a stronger expression of both proteins on methanol and glucose. Atg28 mediated the interaction of Atg35 with Atg17. Trafficking of overexpressed Atg17 from the peripheral ER to the nuclear envelope was required to organize a peri-nuclear structure (PNS), the site of Atg35 colocalization during micropexophagy. In summary, Atg35 is a new Atg protein that relocates to the PNS and specifically regulates MIPA formation during micropexophagy.
机译:自噬相关(Atg)途径将细胞溶胶和细胞器传递到称为自噬体的双膜囊泡中,并在液泡组装位点(PAS)形成,大多数核心Atg蛋白质在此处组装。 Atg28是毕赤酵母中所有Atg途径所必需的核心自噬机制的组成部分。这种盘绕的线圈蛋白与Atg17相互作用,是微石咽症必不可少的。但是,Atg28在微咽病中的作用尚不清楚。我们使用酵母双杂交系统从巴斯德毕赤酵母中搜索Atg28相互作用伴侣,并鉴定了一种新的Atg蛋白,名为Atg35。 atg35Δ突变体在巨石吞噬作用,细胞质-液泡靶向或一般自噬方面不受影响。但是,对于微型咽部疾病和微型咽部器具(MIPA)的形成,都需要Atg28和Atg35。该要求与蛋白质在甲醇和葡萄糖上的更强表达有关。 Atg28介导Atg35与Atg17的相互作用。需要将过表达的Atg17从外围ER转运到核膜,以组织核周围结构(PNS),这是微石吞期间Atg35共定位的部位。总而言之,Atg35是一种新的Atg蛋白,可重新定位到PNS并在微石吞过程中特异性调节MIPA的形成。

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