The scaffolding protein Oskar organizes two types of germ granules by phase transition within the same cell but with distinct morphologies, composition and biological functions.
The protein Pat1 functions in the assembly of processing bodies, cellular membraneless organelles, by promoting the liquid–liquid phase separation of the DEAD-box ATPase Dhh1 and RNA.
CPEB4's switch from translational repressor to activator is regulated during cell cycle by hyperphosphorylation of its intrinsically disordered domain, which controls its phase-separation into RNA-containing liquid-like droplets.
Statistics on the frequencies of pi interactions in folded protein structures enable successful prediction of intrinsically disordered protein phase separation, with clear implications for a physical understanding of cellular organization.
Crosslink immunopreciptiation (iCLIP) studies reveal important mechanistic insights into how MARF1 post-transcriptionally regulates targeted mRNAs and uncover a novel mode by which EDC4 regulates mRNA metabolism.
A trypanosome DYRK kinase that exhibits fundamental differences to conventional DYRK family regulation links parasite quorum sensing, signal transduction and developmental gene expression.
Widespread, rapidly evolving disordered regions contain molecular features that are preserved over evolution and are associated with specific biological functions.
Multi-scale simulations reveal a potential, ATP-independent mechanism resulting in the formation of the long-living multi-droplet state by multi-valent, spacer-sticker proteins.
