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本文引用的文献

1
The Atg1 complex, Atg9, and Vac8 recruit PI3K complex I to the pre-autophagosomal structure.Atg1 复合物、Atg9 和 Vac8 将 PI3K 复合物 I 招募到前自噬体结构。
J Cell Biol. 2023 Aug 7;222(8). doi: 10.1083/jcb.202210017. Epub 2023 Jul 12.
2
Structures of Vac8-containing protein complexes reveal the underlying mechanism by which Vac8 regulates multiple cellular processes.Vac8 包含蛋白复合物的结构揭示了 Vac8 调控多种细胞过程的潜在机制。
Proc Natl Acad Sci U S A. 2023 May 2;120(18):e2211501120. doi: 10.1073/pnas.2211501120. Epub 2023 Apr 24.
3
Spatial control of avidity regulates initiation and progression of selective autophagy.空间控制亲和性调节选择性自噬的起始和进展。
Nat Commun. 2021 Dec 10;12(1):7194. doi: 10.1038/s41467-021-27420-3.
4
Vac8 determines phagophore assembly site vacuolar localization during nitrogen starvation-induced autophagy.Vac8 在氮饥饿诱导的自噬过程中决定吞噬体组装位点的液泡定位。
Autophagy. 2021 Jul;17(7):1636-1648. doi: 10.1080/15548627.2020.1776474. Epub 2020 Jun 17.
5
Vac8 spatially confines autophagosome formation at the vacuole in .Vac8 在液泡处将自噬体的形成局限在 Vac8 区域内。
J Cell Sci. 2019 Nov 14;132(22):jcs235002. doi: 10.1242/jcs.235002.
6
Quaternary structures of Vac8 differentially regulate the Cvt and PMN pathways.Vac8 的四级结构差异调节 Cvt 和 PMN 途径。
Autophagy. 2020 Jun;16(6):991-1006. doi: 10.1080/15548627.2019.1659615. Epub 2019 Sep 12.
7
Unification of Protein Abundance Datasets Yields a Quantitative Saccharomyces cerevisiae Proteome.蛋白质丰度数据集的统一产生了一个定量的酿酒酵母蛋白质组。
Cell Syst. 2018 Feb 28;6(2):192-205.e3. doi: 10.1016/j.cels.2017.12.004. Epub 2018 Jan 17.
8
Mechanistic insight into the nucleus-vacuole junction based on the Vac8p-Nvj1p crystal structure.基于 Vac8p-Nvj1p 晶体结构的核-液泡连接点的机制见解。
Proc Natl Acad Sci U S A. 2017 Jun 6;114(23):E4539-E4548. doi: 10.1073/pnas.1701030114. Epub 2017 May 22.
9
The most important thing is the tail: multitudinous functionalities of intrinsically disordered protein termini.最重要的是尾部:无规卷曲蛋白末端的众多功能。
FEBS Lett. 2013 Jun 27;587(13):1891-901. doi: 10.1016/j.febslet.2013.04.042. Epub 2013 May 10.
10
Intrinsic disorder-based protein interactions and their modulators.基于固有无序的蛋白质相互作用及其调节剂。
Curr Pharm Des. 2013;19(23):4191-213. doi: 10.2174/1381612811319230005.

Vac8(一种在酵母中具有多种功能的犰狳重复蛋白)的新重要性。

The emerging significance of Vac8, a multi-purpose armadillo-repeat protein in yeast.

作者信息

Popelka Hana, Klionsky Daniel J

机构信息

Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA.

出版信息

Autophagy. 2025 May;21(5):913-916. doi: 10.1080/15548627.2024.2377377. Epub 2024 Jul 24.

DOI:10.1080/15548627.2024.2377377
PMID:39045779
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC12013421/
Abstract

Vac8 is the sole armadillo-repeat (ARM) protein in yeast. The function of Vac8 in the cytoplasm-to-vacuole targeting pathway has been known for a long time but its role in the phagophore assembly site localization and recruitment of autophagy-related protein complexes is slowly coming to light. Because Vac8 is also involved in formation of the nuclear-vacuole junction and vacuole inheritance, the protein needs to be a competent and wide-ranging mediator of cellular processes. In this article, we discuss two recent studies reporting on Vac8 and its binding partners. We describe Vac8 in the context of crystallized protein complexes as well as predicted models to reveal the versatility of Vac8 and its potential to become a subject of future autophagy research. ARM, armadillo repeat; Cvt, cytoplasm-to-vacuole targeting; IDPR, intrinsically disordered protein region NVJ, nucleus-vacuole junction; SEC, size-exclusion chromatography.

摘要

Vac8是酵母中唯一的犰狳重复序列(ARM)蛋白。Vac8在细胞质到液泡靶向途径中的功能早已为人所知,但其在吞噬泡组装位点定位和自噬相关蛋白复合物募集方面的作用才逐渐被揭示。由于Vac8还参与核-液泡连接的形成和液泡遗传,该蛋白需要成为细胞过程中能干且广泛的介质。在本文中,我们讨论了两项最近关于Vac8及其结合伴侣的研究。我们在结晶蛋白复合物以及预测模型的背景下描述Vac8,以揭示Vac8的多功能性及其成为未来自噬研究对象的潜力。ARM,犰狳重复序列;Cvt,细胞质到液泡靶向;IDPR,内在无序蛋白区域;NVJ,核-液泡连接;SEC,尺寸排阻色谱法