缺乏信号肽酶复合体非催化亚基 Spc1 的酵母细胞膜蛋白质组的丰度

Chewon Yim, Yeonji Chung, Sungjoon Son, Jeesoo Kim, Jong-Seo Kim, Hyun Kim
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引用次数: 0

摘要

信号肽酶复合体(SPC)介导分泌前体信号肽的处理。但最近的研究表明,真核生物 SPC 还能裂解一些膜蛋白的内部跨膜片段,其非催化亚基 Spc1/SPCS1 在这一过程中发挥着关键作用。为了评估 Spc1 对膜蛋白稳态的影响,我们对含有和不含 Spc1 的酵母细胞进行了定量蛋白质组学研究。我们的数据显示,与野生型细胞相比,缺乏 Spc1 的酵母细胞膜蛋白质组的丰度普遍降低,这表明 Spc1 在控制细胞膜蛋白质水平方面发挥了作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Abundance of the Membrane Proteome in Yeast Cells Lacking Spc1, a Non-catalytic Subunit of the Signal Peptidase Complex

Abundance of the Membrane Proteome in Yeast Cells Lacking Spc1, a Non-catalytic Subunit of the Signal Peptidase Complex

The signal peptidase complex (SPC) mediates processing of signal peptides of secretory precursors. But, recent studies show that the eukaryotic SPC also cleaves internal transmembrane segments of some membrane proteins, and its non-catalytic subunit, Spc1/SPCS1 plays a critical role in this process. To assess the impact of Spc1 on membrane proteostasis, we carried out quantitative proteomics of yeast cells with and without Spc1. Our data show that the abundance of the membrane proteome in yeast cells lacking Spc1 is in general reduced compared to that in wild-type cells, implicating its role in controlling the cellular levels of membrane proteins.

Graphical abstract

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