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酵母细胞中信号肽酶复合物非催化亚基 Spc1 缺失时膜蛋白组的丰度。

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

机构信息

School of Biological Sciences and Institute of Microbiology, Seoul National University, Building 504-421, Seoul, 08826, South Korea.

Center for RNA Research, Institute for Basic Science, Seoul, 08826, South Korea.

出版信息

J Membr Biol. 2024 Aug;257(3-4):207-214. doi: 10.1007/s00232-024-00312-5. Epub 2024 Apr 17.

DOI:10.1007/s00232-024-00312-5
PMID:38630294
Abstract

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.

摘要

信号肽酶复合物(SPC)介导分泌前体的信号肽的加工。但是,最近的研究表明,真核 SPC 也切割一些膜蛋白的内部跨膜片段,其非催化亚基 Spc1/SPCS1 在这个过程中起着关键作用。为了评估 Spc1 对膜蛋白稳态的影响,我们对有和没有 Spc1 的酵母细胞进行了定量蛋白质组学研究。我们的数据表明,与野生型细胞相比,缺乏 Spc1 的酵母细胞中膜蛋白组的丰度通常降低,这表明它在控制膜蛋白的细胞水平方面发挥作用。

相似文献

1
Abundance of the Membrane Proteome in Yeast Cells Lacking Spc1, a Non-catalytic Subunit of the Signal Peptidase Complex.酵母细胞中信号肽酶复合物非催化亚基 Spc1 缺失时膜蛋白组的丰度。
J Membr Biol. 2024 Aug;257(3-4):207-214. doi: 10.1007/s00232-024-00312-5. Epub 2024 Apr 17.
2
Spc1 regulates the signal peptidase-mediated processing of membrane proteins.Spc1 调节信号肽酶介导的膜蛋白加工。
J Cell Sci. 2021 Jul 1;134(13). doi: 10.1242/jcs.258936. Epub 2021 Jul 9.
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Combining Deep Sequencing, Proteomics, Phosphoproteomics, and Functional Screens To Discover Novel Regulators of Sphingolipid Homeostasis.结合深度测序、蛋白质组学、磷酸化蛋白质组学和功能筛选以发现鞘脂稳态的新型调节因子。
J Proteome Res. 2017 Feb 3;16(2):571-582. doi: 10.1021/acs.jproteome.6b00691. Epub 2016 Nov 29.
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The homologue of mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae.哺乳动物SPC12的同源物对酿酒酵母中高效信号肽酶活性很重要。
J Biol Chem. 1996 Jul 12;271(28):16460-5. doi: 10.1074/jbc.271.28.16460.
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Signal peptidase I processed secretory signal sequences: Selection for and against specific amino acids at the second position of mature protein.信号肽酶I处理的分泌信号序列:成熟蛋白第二位特定氨基酸的正负选择。
Biochem Biophys Res Commun. 2017 Feb 12;483(3):972-977. doi: 10.1016/j.bbrc.2017.01.044. Epub 2017 Jan 11.
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The yeast SPC22/23 homolog Spc3p is essential for signal peptidase activity.酵母SPC22/23同源物Spc3p对信号肽酶活性至关重要。
J Biol Chem. 1997 May 16;272(20):13159-64. doi: 10.1074/jbc.272.20.13159.
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Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct.酵母信号肽酶复合体中结构相关的Spc1p和Spc2p在功能上是不同的。
J Biol Chem. 1996 Nov 15;271(46):29094-9. doi: 10.1074/jbc.271.46.29094.
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Membrane topology and biogenesis of eukaryotic signal peptidase.真核信号肽酶的膜拓扑结构与生物发生
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Genetic complementation in yeast reveals functional similarities between the catalytic subunits of mammalian signal peptidase complex.酵母中的基因互补揭示了哺乳动物信号肽酶复合体催化亚基之间的功能相似性。
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Signal peptidase complex subunit 1 participates in the assembly of hepatitis C virus through an interaction with E2 and NS2.信号肽酶复合体亚基 1 通过与 E2 和 NS2 的相互作用参与丙型肝炎病毒的组装。
PLoS Pathog. 2013;9(8):e1003589. doi: 10.1371/journal.ppat.1003589. Epub 2013 Aug 29.

本文引用的文献

1
Mechanisms of substrate processing during ER-associated protein degradation.内质网相关蛋白降解过程中底物加工的机制。
Nat Rev Mol Cell Biol. 2023 Nov;24(11):777-796. doi: 10.1038/s41580-023-00633-8. Epub 2023 Aug 1.
2
The human signal peptidase complex acts as a quality control enzyme for membrane proteins.人信号肽酶复合体能作为膜蛋白的质量控制酶。
Science. 2022 Dec 2;378(6623):996-1000. doi: 10.1126/science.abo5672. Epub 2022 Dec 1.
3
Endoplasmic Reticulum-Associated Protein Degradation.内质网相关蛋白降解。
Cold Spring Harb Perspect Biol. 2022 Dec 1;14(12):a041247. doi: 10.1101/cshperspect.a041247.
4
Spc1 regulates the signal peptidase-mediated processing of membrane proteins.Spc1 调节信号肽酶介导的膜蛋白加工。
J Cell Sci. 2021 Jul 1;134(13). doi: 10.1242/jcs.258936. Epub 2021 Jul 9.
5
Delayed by Design: Role of Suboptimal Signal Peptidase Processing of Viral Structural Protein Precursors in Flaviviridae Virus Assembly.设计使然:结构蛋白前体信号肽酶切不成熟在黄病毒科病毒装配中的作用。
Viruses. 2020 Sep 26;12(10):1090. doi: 10.3390/v12101090.
6
SignalP 5.0 improves signal peptide predictions using deep neural networks.SignalP 5.0 使用深度神经网络改进了信号肽预测。
Nat Biotechnol. 2019 Apr;37(4):420-423. doi: 10.1038/s41587-019-0036-z. Epub 2019 Feb 18.
7
Murine astrotactins 1 and 2 have a similar membrane topology and mature via endoproteolytic cleavage catalyzed by a signal peptidase.鼠脑星状蛋白 1 和 2 具有相似的膜拓扑结构,并通过信号肽酶催化的内肽切割成熟。
J Biol Chem. 2019 Mar 22;294(12):4538-4545. doi: 10.1074/jbc.RA118.007093. Epub 2019 Jan 29.
8
Membrane Protein Quantity Control at the Endoplasmic Reticulum.内质网的膜蛋白数量控制
J Membr Biol. 2017 Aug;250(4):379-392. doi: 10.1007/s00232-016-9931-0. Epub 2016 Oct 14.
9
A CRISPR screen defines a signal peptide processing pathway required by flaviviruses.一项CRISPR筛选确定了黄病毒所需的信号肽加工途径。
Nature. 2016 Jul 7;535(7610):164-8. doi: 10.1038/nature18625. Epub 2016 Jun 17.
10
A forward genetic screen reveals novel independent regulators of ULBP1, an activating ligand for natural killer cells.一项正向遗传学筛选揭示了ULBP1(一种自然杀伤细胞激活配体)新的独立调节因子。
Elife. 2015 Nov 13;4:e08474. doi: 10.7554/eLife.08474.