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| Item Type: | Article |
|---|---|
| Title: | Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules |
| Creators Name: | Cipriani, P.G., Bay, O., Zinno, J., Gutwein, M., Gan, H.H., Mayya, V.K., Chung, G., Chen, J.X., Fahs, H., Guan, Y., Duchaine, T.F., Selbach, M., Piano, F. and Gunsalus, K.C. |
| Abstract: | We describe MIP-1 and MIP-2, novel paralogous C. elegans germ granule components that interact with the intrinsically disordered MEG-3 protein. These proteins promote P granule condensation, form granules independently of MEG-3 in the postembryonic germ line, and balance each other in regulating P granule growth and localization. MIP-1 and MIP-2 each contain two LOTUS domains and intrinsically disordered regions and form homo- and heterodimers. They bind and anchor the Vasa homolog GLH-1 within P granules and are jointly required for coalescence of MEG-3, GLH-1, and PGL proteins. Animals lacking MIP-1 and MIP-2 show temperature-sensitive embryonic lethality, sterility, and mortal germ lines. Germline phenotypes include defects in stem cell self-renewal, meiotic progression, and gamete differentiation. We propose that these proteins serve as scaffolds and organizing centers for ribonucleoprotein networks within P granules that help recruit and balance essential RNA processing machinery to regulate key developmental transitions in the germ line. |
| Keywords: | P Granules, Germline, Stem Cell Niche, Embryogenesis, LOTUS, OST-HTH, Oskar, GLH-1, Vasa, IDR, Liquid-Liquid Phase Separation, Biomolecular Condensate, Animals, Caenorhabditis elegans |
| Source: | eLife |
| ISSN: | 2050-084X |
| Publisher: | eLife Sciences Publications |
| Volume: | 10 |
| Page Range: | e60833 |
| Date: | 3 August 2021 |
| Official Publication: | https://doi.org/10.7554/eLife.60833 |
| PubMed: | View item in PubMed |
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