Biology subjects

Price, I. F.

Publications and source records attributed to Price, I. F..

3 recordsLinked to original sources

bioRxiv2026

LOTUS-domain proteins activate Vasa to drive germ granule assembly

Germline development relies on perinuclear membraneless germ granules, yet the mechanisms underlying their assembly remain incompletely understood. Here we uncover a conserved and central role for LOTUS-domain proteins in driving germ granule assembly. In C. elegans, the LOTUS-domain protein EGGD-1/MIP-1 at sub-stoichiometric levels recruits Vasa protein GLH-1 to the nuclear periphery. Acting as a catalyst, EGGD-1 impacts the ATPase cycles of GLH-1 by preferentially binding to its open conformation, enhancing its RNA binding activities, and facilitating its transition to the closed conformation. GLH-1 in the closed state enriches mRNAs at the nuclear periphery, which enables the accumulation of RNA-binding proteins including PGL-1 and PGL-3. Using human cells, we demonstrate the LOTUS-domain protein TDRD5 similarly recruits DDX4, the human Vasa homolog, and stimulates the formation of intermitochondrial cement. Collectively, these findings reveal evolutionarily conserved stimulatory effect of LOTUS-domain protein in Vasa activity and provide a unified model for germ granule assembly across species.

cell biology↗

bioRxiv2025

Kinetochore components are perinuclear and form condensates in C. elegans germline

The kinetochore is a multiprotein complex that assembles on centromeric chromatin and serves as the attachment site for spindle microtubules, thereby ensuring accurate chromosome segregation during cell division. Here we present evidence that kinetochore components, such as HCP-1, form distinct cytoplasmic foci in the C. elegans germline. Prior to cell division, HCP-1 localizes to the nuclear envelope of germ nuclei and forms granules that are distinct from germ granules. Upon mitotic entry, perinuclear HCP-1 is imported into the nucleus to facilitate chromosome segregation. We further show that HCP-1 associates with nuclear pore proteins (NPPs). Loss of NPP-14 disperses perinuclear HCP-1, impairs its nuclear import, and leads to defects in germ cell proliferation and embryonic spindle assembly. Together, these findings provide new insights into the spatial regulation of kinetochore components and their roles in nuclear organization.

cell biology↗

bioRxiv2021

Proximity labeling identifies LOTUS domain proteins that promote the formation of perinuclear germ granules in C. elegans

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.

cell biology↗