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.
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No datasets were generated or analyzed during the current study.
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Funding
This work was supported by a grant from the National Research Foundation of Korea (NRF-2022R1A2C1010060) to Hyun Kim and supported by the Institute for Basic Science from the Ministry of Science and Information and Communications Technology of Korea (IBS-R008-D1) to Jeesoo Kim and Jong-Seo Kim.
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CY, YC and HK conceptualized research; CY, YC and SS performed experiments using yeast cells; JK and J-SK performed quantitative mass spectrometry and analyzed data; CY, YC and HK analyzed experimental data and wrote the paper; CY, YC, SS, JK, J-SK and HK read and edited the manuscript.
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Yim, C., Chung, Y., Son, S. et al. Abundance of the Membrane Proteome in Yeast Cells Lacking Spc1, a Non-catalytic Subunit of the Signal Peptidase Complex. J Membrane Biol (2024). https://doi.org/10.1007/s00232-024-00312-5
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DOI: https://doi.org/10.1007/s00232-024-00312-5