| Source (authors, year) | Venue | Publication date | URL/DOI | What it shows about PGL-1 (localization/function) | Quantitative/statistical findings (if any) |
|---|---|---|---|---|---|
| Price et al., 2023 | *Nature Communications* | Sep 2023 | https://doi.org/10.1038/s41467-023-41556-4 | Identifies PGL-1 as an RNA-binding scaffold protein enriched in perinuclear P granules of the *C. elegans* germline. Shows that perinuclear organization depends on EGGD-1/GLH-1, and that disruption of this architecture causes PGL-1 mislocalization into abnormal cytoplasmic/rachis aggregates and perturbs small-RNA pathway organization and RNAome control. (pqac-00000000, pqac-00000004) | In *eggd-1* mutants, mean PGL-1::RFP granule volume at the nuclear membrane decreased from 0.482 to 0.183 µm3 (2.64-fold smaller), while rachis-associated PGL-1::RFP increased to 0.947 µm3; some cytoplasmic foci reached ~25 µm3. PGL-1::GFP mean perinuclear volume decreased from 0.332 to 0.120 µm3 (2.77-fold). (pqac-00000000) |
| Uebel et al., 2023 | *Development* | Dec 2023 | https://doi.org/10.1242/dev.202284 | Describes PGL-1 as a major constituent of perinuclear, phase-separated P granules and uses high-resolution imaging to define P-granule architecture. Reports toroidal "P granule pockets" and supports a hierarchical model in which P granules organize other nuage compartments around nuclear pores, shaping RNA surveillance as transcripts exit the nucleus. (pqac-00000002, pqac-00000007) | Figure-based quantification reported an average of 22.4 ± 3.6 perinuclear P granules per nucleus, alongside stoichiometric distributions of P-granule populations associated with other nuage compartments. (pqac-00000007) |
| Zheng et al., 2023 | *Journal of Cell Biology* | Apr 2023 | https://doi.org/10.1083/jcb.202210104 | Shows that PGL-1 is a core P-granule protein that forms RNA-containing condensates with PGL-3 and SEPA-1. RNAs promote LLPS/liquidity of these condensates, recruit translation/RNA-control factors, and shift granules away from autophagic degradation toward accumulation under stress. Also notes PGL-1 interaction with IFE-1 and strong IFE-1 localization to germline P granules. (pqac-00000001, pqac-00000003) | In vitro assays used purified PGL-1/PGL-3/SEPA-1 at 3 µM each; adding 10–30 ng/µl mRNA enlarged condensates and accelerated fusion/relaxation. Approximately 68% of PGL granules were IFE-1-positive. PGL granules appeared by the ~20-cell embryonic stage and increased in number at 26°C. (pqac-00000001, pqac-00000003) |
| Huang et al., 2024 preprint / 2025 bioRxiv posting | *bioRxiv* | Preprint posted Mar 2025; DOI indicates initial 2024 deposition | https://doi.org/10.1101/2024.03.25.586584 | Uses PGL-1::tagRFP as the canonical marker for P granules in systematic colocalization mapping of germ-granule subcompartments. Table annotations describe PGL-1 as a P-granule-localized endoribonuclease, and imaging places it in perinuclear P granules relative to PRG-1, ZNFX-1, DDX-19, and other compartment markers. The study is primarily a localization/resource paper rather than a direct mechanistic dissection of PGL-1 catalysis. (pqac-00000005, pqac-00000006) | The cited excerpts emphasize fluorescence line-scan colocalization analyses rather than phenotype statistics; no direct quantitative fertility or RNAome values for PGL-1 were provided in the retrieved sections. (pqac-00000005, pqac-00000006) |


*Table: This table summarizes key recent papers and a relevant preprint on *C. elegans* PGL-1, focusing on localization, function, and quantitative findings. It is useful for quickly distinguishing direct evidence on P-granule biology from marker/localization studies.*