| Year (month) | Citation (first author et al.) | Title (short) | Study type | Key SEC11C-relevant takeaways | URL (DOI) |
|---|---|---|---|---|---|
| 2015 (Nov) | Cui et al. | Competitive inhibition of ER signal peptidase | inhibitor/antiviral | Defines mammalian ER signal peptidase as a five-subunit complex including SEC11C and SEC11A; supports the catalytic importance of SEC11-family subunits and shows that blocking signal peptidase impairs maturation of secretory and viral proteins, motivating host-targeted antiviral interest (pqac-00000008). | https://doi.org/10.1074/jbc.m115.692350 |
| 2021 (Jan) | Liaci et al. | Human SPC structure and signal peptide cleavage determinants | structure/mechanism | Structural anchor for human SEC11C: shows two human SPC paralogs, SPC-A and SPC-C, each with either SEC11A or SEC11C plus SPC12/SPC22-23/SPC25; supports a Ser-His-Asp catalytic triad, luminal catalytic domain, ER-membrane-proximal active site, and local membrane thinning that helps discriminate signal peptides by hydrophobic segment length; SEC11C-containing SPC is active in vitro (pqac-00000000, pqac-00000001, pqac-00000002, pqac-00000009). | https://doi.org/10.2139/ssrn.3778304 |
| 2022 (Dec) | Zanotti et al. | Human SPC as membrane-protein quality control enzyme | QC | Expands SPC biology beyond canonical signal peptide removal: identifies a post-translocational QC role in cleaving cryptic sites in misfolded or surplus membrane proteins and coupling this to ERAD; reports ~1,500 membrane proteins with putative cryptic SPC cleavage sites and notes SEC11A knockdown can be buffered by SEC11C, implying paralog redundancy in mammalian cells (pqac-00000013, pqac-00000014, pqac-00000015, pqac-00000019, pqac-00000020, pqac-00000023). | https://doi.org/10.1126/science.abo5672 |
| 2023 (Jan) | Zanotti | Characterisation of the human SPC as a QC enzyme | QC / subunit function | Thesis-level expansion of the 2022 Science study: states the catalytic core is formed by SEC11A/C with SPCS3, proposes SEC11C may serve as a backup catalytic subunit when SEC11A is limiting, and notes SEC11C is often hard to detect in some cell lines with normal SEC11A levels; cavinafungin is discussed as likely inhibiting SEC11C as well as SEC11A (pqac-00000003, pqac-00000004, pqac-00000016, pqac-00000017, pqac-00000021, pqac-00000022). | https://doi.org/10.11588/heidok.00033417 |
| 2024 (Nov) | Chung et al. | Spc2 modulates substrate and cleavage-site selection | subunit function / mechanism | Although performed in yeast, this recent mechanistic study is relevant to human SEC11C because it explicitly frames higher-eukaryote SPC as a heterotetramer containing SEC11A or SEC11C and shows how accessory subunits shape substrate and cleavage-site selection, reinforcing that catalytic SEC11 paralogs act within a coordinated multi-subunit membrane-thinning machine rather than alone (pqac-00000007). | https://doi.org/10.1083/jcb.202211035 |


*Table: This table summarizes the main publications needed to annotate human SEC11C in context of the signal peptidase complex. It highlights the structural basis, quality-control function, subunit redundancy, and translational relevance of SEC11C/SPC across foundational and recent studies.*