Syntaxin-5 在 SNARE 配对中的灵活性支持高尔基体的功能。

IF 3.6 3区 生物学 Q3 CELL BIOLOGY Traffic Pub Date : 2023-08-01 Epub Date: 2023-06-21 DOI:10.1111/tra.12903
Zinia D'Souza, Irina Pokrovskaya, Vladimir V Lupashin
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引用次数: 0

摘要

保守的寡聚高尔基体(COG)复合体能协调SNARE介导的囊泡的系留/融合,这些囊泡能循环利用高尔基体的糖基化机制,缺乏这种复合体会导致严重的糖基化缺陷。虽然COG缺陷细胞中的两个主要高尔基体v-SNARE--GS28/GOSR1和GS15/BET1L被耗尽,但完全敲除GS28和GS15对高尔基体糖基化的影响不大,这表明高尔基体SNARE存在一种适应机制。事实上,对与 STX5 相互作用的蛋白质进行的定量质谱分析发现了两种新型高尔基体 SNARE 复合物--STX5/SNAP29/VAMP7 和 STX5/VTI1B/STX8/YKT6。这些复合物存在于野生型细胞中,但在 GS28 和 COG 缺陷细胞中的使用率显著增加。删除 GS28 后,SNAP29 会以 STX5 依赖性方式增加其高尔基驻留。STX5 缺失和 Retro2- 诱导的高尔基体分流严重影响了蛋白质糖基化,而 GS28/SNAP29 和 GS28/VTI1B 双基因敲除对糖基化的改变与 GS28 KO 相似,这表明基于 STX5 的单一 SNARE 复合物足以支持高尔基体糖基化。重要的是,在 GS28/SNAP29/VTI1B TKO 细胞中同时缺失三种高尔基体 SNARE 复合物会导致严重的糖基化缺陷,并降低糖基化酶在高尔基体的保留能力。这项研究证明了 SXT5 介导的膜贩运具有显著的可塑性,揭示了对高尔基体内典型囊泡系留/融合机制失效的一种新的适应性反应。
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Syntaxin-5's flexibility in SNARE pairing supports Golgi functions.

Deficiency in the conserved oligomeric Golgi (COG) complex that orchestrates SNARE-mediated tethering/fusion of vesicles that recycle the Golgi's glycosylation machinery results in severe glycosylation defects. Although two major Golgi v-SNAREs, GS28/GOSR1, and GS15/BET1L, are depleted in COG-deficient cells, the complete knockout of GS28 and GS15 only modestly affects Golgi glycosylation, indicating the existence of an adaptation mechanism in Golgi SNARE. Indeed, quantitative mass-spectrometry analysis of STX5-interacting proteins revealed two novel Golgi SNARE complexes-STX5/SNAP29/VAMP7 and STX5/VTI1B/STX8/YKT6. These complexes are present in wild-type cells, but their usage is significantly increased in both GS28- and COG-deficient cells. Upon GS28 deletion, SNAP29 increased its Golgi residency in a STX5-dependent manner. While STX5 depletion and Retro2-induced diversion from the Golgi severely affect protein glycosylation, GS28/SNAP29 and GS28/VTI1B double knockouts alter glycosylation similarly to GS28 KO, indicating that a single STX5-based SNARE complex is sufficient to support Golgi glycosylation. Importantly, co-depletion of three Golgi SNARE complexes in GS28/SNAP29/VTI1B TKO cells resulted in severe glycosylation defects and a reduced capacity for glycosylation enzyme retention at the Golgi. This study demonstrates the remarkable plasticity in SXT5-mediated membrane trafficking, uncovering a novel adaptive response to the failure of canonical intra-Golgi vesicle tethering/fusion machinery.

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来源期刊
Traffic
Traffic 生物-细胞生物学
CiteScore
8.10
自引率
2.20%
发文量
50
审稿时长
2 months
期刊介绍: Traffic encourages and facilitates the publication of papers in any field relating to intracellular transport in health and disease. Traffic papers span disciplines such as developmental biology, neuroscience, innate and adaptive immunity, epithelial cell biology, intracellular pathogens and host-pathogen interactions, among others using any eukaryotic model system. Areas of particular interest include protein, nucleic acid and lipid traffic, molecular motors, intracellular pathogens, intracellular proteolysis, nuclear import and export, cytokinesis and the cell cycle, the interface between signaling and trafficking or localization, protein translocation, the cell biology of adaptive an innate immunity, organelle biogenesis, metabolism, cell polarity and organization, and organelle movement. All aspects of the structural, molecular biology, biochemistry, genetics, morphology, intracellular signaling and relationship to hereditary or infectious diseases will be covered. Manuscripts must provide a clear conceptual or mechanistic advance. The editors will reject papers that require major changes, including addition of significant experimental data or other significant revision. Traffic will consider manuscripts of any length, but encourages authors to limit their papers to 16 typeset pages or less.
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