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Novel LOTUS-domain proteins are organizational hubs that recruit C. elegans Vasa to germ granules

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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. and Bay, O. and Zinno, J. and Gutwein, M. and Gan, H.H. and Mayya, V.K. and Chung, G. and Chen, J.X. and Fahs, H. and Guan, Y. and Duchaine, T.F. and Selbach, M. and 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
Publisher:eLife Sciences Publications
Page Range:e60833
Date:3 August 2021
Official Publication:https://doi.org/10.7554/eLife.60833
PubMed:View item in PubMed
Related to:
https://edoc.mdc-berlin.de/20369/Preprint version

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