Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically-disordered proteins in C. elegans
- Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, United States
- Academica Sinica, Taiwan
- Janelia Farm Research Campus, Howard Hughes Medical Institute, United States
Abstract
RNA granules have been likened to liquid droplets whose dynamics depend on the controlled dissolution and condensation of internal components. The molecules and reactions that drive these dynamics in vivo are not well understood. Here, we present evidence that a group of intrinsically-disordered, serine-rich proteins regulate the dynamics of P granules in C. elegans embryos. The MEG (maternal-effect germline defective) proteins are germ plasm components that are required redundantly for fertility. We demonstrate that MEG-1 and MEG-3 are substrates of the kinase MBK-2/DYRK and the phosphatase PP2APPTR-1/2. Phosphorylation of the MEGs promotes granule disassembly and dephosphorylation promotes granule assembly. Using lattice light sheet microscopy on live embryos, we show that GFP-tagged MEG-3 localizes to a dynamic domain that surrounds and penetrates each granule. We conclude that, despite their liquid-like behavior, P granules are non-homogeneous structures whose assembly in embryos is regulated by phosphorylation.
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© 2014, Wang et al.
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Regulation of RNA granule dynamics by phosphorylation of serine-rich, intrinsically-disordered proteins in C. elegans
eLife 3:e04591.
https://doi.org/10.7554/eLife.04591
