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

Chewon Yim; Yeonji Chung; Sungjoon Son; Jeesoo Kim; Jong-Seo Kim; Hyun Kim

doi:10.1007/s00232-024-00312-5

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

J Membr Biol. 2024 Apr 17. doi: 10.1007/s00232-024-00312-5. Online ahead of print.

Authors

Chewon Yim^#¹, Yeonji Chung^#¹, Sungjoon Son¹, Jeesoo Kim^{1

2}, Jong-Seo Kim^{1

2}, Hyun Kim³

Affiliations

¹ School of Biological Sciences and Institute of Microbiology, Seoul National University, Building 504-421, Seoul, 08826, South Korea.
² Center for RNA Research, Institute for Basic Science, Seoul, 08826, South Korea.
³ School of Biological Sciences and Institute of Microbiology, Seoul National University, Building 504-421, Seoul, 08826, South Korea. joy@snu.ac.kr.

^# Contributed equally.

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

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.

Keywords: Membrane proteins; Quality control; Quantity control; SPCS1; Spc12.

Abstract

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