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 PMID:34223818  

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

Patricia Giselle Cipriani | Olivia Bay | John Zinno | Michelle Gutwein | Hin Hark Gan | Vinay K Mayya | George Chung | Jia-Xuan Chen | Hala Fahs | Yu Guan | Thomas F Duchaine | Matthias Selbach | Fabio Piano | Kristin C Gunsalus
eLife | 2021

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.

Pubmed ID: 34223818

Associated grants

  • Agency: CIHR, Canada
    Id: MOP 123352
  • Agency: NIH HHS, United States
    Id: P40 OD010440

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

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