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Organelles without membranes: intrinsically‐disordered proteins bring order to the cytoplasm

RNA granules are non‐membrane bound cellular compartments that contain RNA and RNA binding proteins. The molecular mechanisms that regulate the spatial distribution of RNA granules in cells are poorly understood. During polarization of the C. elegans zygote, germline RNA granules, called P granules, assemble preferentially in the posterior cytoplasm. We have identified two intrinsically disordered proteins MEG‐3 and MEG‐4 that function redundantly to scaffold the assembly of P granules in the posterior cytoplasm. We will describe how MEG‐3 and MEG‐4's ability to phase separate with RNA, bind to other RNA‐binding proteins, and be phosphorylated by DYRK MBK‐2 contribute to localized P granule assembly.