bioRxivCell Biology
Proximity labeling identifies LOTUS domain proteins that promote the formation of perinuclear germ granules in C. elegans
Abstract
The germline produces gametes that transmit genetic and epigenetic information to the next generation. Maintenance of germ cells and development of gametes require germ granules--well-conserved membraneless and RNA-rich organelles. The composition of germ granules is elusive owing to their dynamic nature and their exclusive expression in the germline. Using C. elegans germ granule, called P granule, as a model system, we employed a proximity-based labeling method in combination with mass spectrometry to comprehensively define its protein components. This set of experiments identified over 200 proteins, many of which contain intrinsically disordered regions. An RNAi-based screen identified factors that are essential for P granule assembly, notably EGGD-1 and EGGD-2, two previously uncharacterized LOTUS-domain proteins. Loss of eggd-1 and eggd-2 results in separation of P granules from nuclear envelope, germline atrophy and reduced fertility. We show that intrinsically disordered regions of EGGD-1 are required to anchor EGGD-1 to the nuclear periphery while its LOTUS domains are required to promote perinuclear localization of P granules. Together, our work expands the repertoire of P granule constituents and provides new insights into the role of LOTUS-domain proteins in germ granule organization.
- organism: C. elegans
- assay: proteomics
- research focus: cell type annotation
- approach: experimental assay
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Compartmentalized localization of perinuclear proteins within germ granules in C. elegans
Xiaona Huang, Xuezhu Feng, … Xiangyang Chen·Developmental CellPeer-reviewed·Dec 31, 2024
- LOTUS-domain proteins activate Vasa to drive germ granule assembly
Ian F. Price, Chin Wang, Wen Tang·bioRxiv·Jan 9, 2026
- Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules
P. G. Cipriani, O. Bay, … K. Gunsalus·bioRxiv·Jun 17, 2021
- Expansion microscopy reveals subdomains in C. elegans germ granules
K. M. Suen, T. M. D. Sheard, … J. E. Ladbury·bioRxiv·May 29, 2022
- TurboID-based proximity labeling identifies novel germline proteins that maintain E granule integrity and small RNA homeostasis in C. elegans
Kun Li, Xuezhu Feng, … Xiangyang Chen·Science China Life SciencesPeer-reviewed·Oct 10, 2025
- Germline RNA helicases couple RNA binding to P granule assembly at nuclear periphery