IF 3.5 4区 生物学 Q1 Biochemistry, Genetics and Molecular Biology
Jordan Thompson, François-Michel Boisvert, Jayme Salsman, Dominique Lévesque, Graham Dellaire, Neale D Ridgway
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引用次数: 0

摘要

早幼粒细胞白血病(PML)蛋白构成了PML核体(PML NB)的支架,在脂肪酸胁迫下,PML核体重组为脂质相关PML结构(LAPS)。通过在 U2OS 细胞中表达与抗坏血酸过氧化物酶 APEX2 的融合,我们确定了脂肪酸油酸如何改变 PMLI 或 PMLII 的相互作用组。由此产生的相互作用组包括ESCRT和COPII转运蛋白节点。近接试验(PLA)显示,COPII蛋白SEC23B、SEC24A和USO1优先与PML NB相关。在 PML 基因敲除细胞中,USO1(而非 SEC23B 和 SEC24A)的核定位减少,而通过表达 PMLII 则可恢复。因此,近距离标记方法确定了 COPII 运输蛋白与 PML NB 的相互作用,这种相互作用会因脂肪酸胁迫而中断。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The proximity interactome of PML isoforms I and II under fatty acid stress.

Promyelocytic leukemia (PML) protein forms the scaffold for PML nuclear bodies (PML NB) that reorganize into Lipid-Associated PML Structures (LAPS) under fatty acid stress. We determined how the fatty acid oleate alters the interactome of PMLI or PMLII by expressing fusions with the ascorbate peroxidase APEX2 in U2OS cells. The resultant interactome included ESCRT and COPII transport protein nodes. Proximity ligation assay (PLA) revealed that COPII proteins SEC23B, SEC24A and USO1 preferentially associated with PML NBs. Nuclear localization of USO1, but not SEC23B and SEC24A, was reduced in PML knockout cells and restored by PMLII expression. Thus, proximity-labelling methods identified COPII transport protein interactions with PML NBs that are disrupted by fatty acid stress.

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来源期刊
FEBS Letters
FEBS Letters 生物-生化与分子生物学
CiteScore
7.00
自引率
2.90%
发文量
303
审稿时长
1.0 months
期刊介绍: FEBS Letters is one of the world''s leading journals in molecular biology and is renowned both for its quality of content and speed of production. Bringing together the most important developments in the molecular biosciences, FEBS Letters provides an international forum for Minireviews, Research Letters and Hypotheses that merit urgent publication.
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