TY - JOUR T1 - Novel LOTUS-domain proteins are organizational hubs that recruit <em>C. elegans</em> Vasa to germ granules JF - bioRxiv DO - 10.1101/2021.06.17.448425 SP - 2021.06.17.448425 AU - P. Giselle Cipriani AU - Olivia Bay AU - John Zinno AU - Michelle Gutwein AU - Hin Hark Gan AU - Vinay K. Mayya AU - George Chung AU - Jia-Xuan Chen AU - Hala Fahs AU - Yu Guan AU - Thomas F. Duchaine AU - Matthias Selbach AU - Fabio Piano AU - Kristin C. Gunsalus Y1 - 2021/01/01 UR - http://biorxiv.org/content/early/2021/06/17/2021.06.17.448425.abstract N2 - 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.Competing Interest StatementThe authors have declared no competing interest. ER -