Phase diagrams for 140 variants of prion-like low-complexity domains are computed to establish scaling laws that quantify the impact of amino acid mutations on the thermodynamic stability of condensates.

Biophysical binding and structural prediction studies reveal that Tetraspanin12 directly binds the ligand Norrin, in a manner that is negatively cooperative with Norrin-Fzd4 binding and competitive with Norrin-LRP5/6 binding.

Gradual downregulation of each of the subunits of the evolutionary-conserved exocyst holocomplex shows that the complex is required for biogenesis, maturation, and exocytosis of secretory granules in Drosophila salivary glands.