Proteomics identifies substrates and a novel component in hSnd2-dependent ER protein targeting
Open accessPreprint — published as 10.3390/cells11182925 · Paper page
Abstract
SUMMARY: Protein import into the endoplasmic reticulum (ER) is essential for about 30% of the human proteome. It involves targeting of precursor proteins to the ER and insertion into or translocation across the ER membrane. Furthermore, it relies on signals in the precursor polypeptides and components, which read the signals and facilitate their targeting to a protein-conducting channel in the ER membrane, the Sec61 complex. Compared to the SRP- and TRC-dependent pathways, little is known about the SRP-independent/SND pathway. Our aim was to identify additional components and characterize the client spectrum of the human SND pathway. The established strategy of combining depletion of the central hSnd2-component from HeLa cells with proteomic- and differential protein abundance-analysis was used. The SRP and TRC targeting pathways were analyzed in comparison. TMEM109 was characterized as hSnd3. Unlike SRP but similar to TRC, the SND clients are predominantly membrane proteins with N-terminal, central, or C-terminal targeting signals.
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- Authors
- Tirincsi, A., O’Keefe, S., Nguyen, D., Sicking, M., Dudek, J., Förster, F., Jung, M., Hadzibeganovic, D., Helms, V., High, S., Zimmermann, R., & Lang, S.
- Affiliations
- Saarland University (DE)
- University of Manchester (GB)
- Utrecht University (NL)
- Corresponding author
- Zimmermann, Richard
- Lang, Sven
- ORCID
- Venue
- bioRxiv (Cold Spring Harbor Laboratory)
- Publisher
- openRxiv
- Published
- 2022-04-27
- OpenAlex
- W4225140264
- Cited by
- 7
- References
- 4
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 1 · 2022: 4
- Type
- posted content
- Language
- en
- Open access
- green
- doi.org
- Locations
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
- Työväentutkimus Vuosikirja (submittedVersion)
- Publications of the UdS (Saarland University) (cc-by)
- Funders
- Wellcome Trust (204957/Z/16/Z)
- Deutsche Forschungsgemeinschaft (SFB 894, ZI 234/13-1, IRTG 1830, FO716/4-1, HE3875/15-1, 204957/Z/16/Z)
- Universität des Saarlandes
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- Sec61, client proteins, HeLa cells
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