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

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

Blog Article

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 Anti-Perspirant 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 L-Glutathione 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.