1 RNA-binding and prion domains: the Yin and Yang of phase separation

Prion-Like Domains (PrLDs)
and RNA-binding domains (RBDs).

We found that one PrLD is sufficient to drive PS, whereas multiple RBDs are needed to modulate the dynamics of the assemblies. （一个PrLD对于相变已经充足，然而我们需要多个RBDs来调节组装的动态）

In the case of stress granule protein Pub1 we show that the PrLD promotes sequestration of protein partners and the RBD confers liquid-like behaviour to the condensate. （在应激颗粒蛋白Pub1的情况下，我们表明，PrLD促进蛋白质伙伴的封存，RBD赋予冷凝液类似液体的行为）

相变的发生不一定要很多蛋白伙伴，但是需要很多RBDs来赋予液体特征

PLAAC analysis：Prion-like amino acid composition (PLAAC)
catGRANULE :(available at http://s.tartaglialab.com/new submission/catGRANULE) was employed to identify proteins assembling into biological condensates.

2 Hsp27 chaperones FUS phase separation under the modulation of stress-induced phosphorylation

Protein phase separation drives the assembly of membraneless organelles, but little is known about how these membraneless organelles are maintained in a metastable liquid- or gel-like phase rather than proceeding to solid aggregation. （蛋白质相分离推动了无膜细胞器的组装，但对于这些无膜细胞器如何维持在可转移的液态或凝胶状相中，而不是进行固体聚集，却知之甚少。）

文献

1 Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation（https://doi.org/10.1016/j.cell.2018.03.004）

（1） TDP-43 and FUS are enriched in the cell nucleus, but in post mortem brains and spinal cords of ALS/FTD patients, they are often absent from the nucleus and are found in cytoplasmic aggregates in neuronal and sometimes glia cells （TDB-43 与FUS一般情况下回聚集在细胞核中，但是在ALS/FTD患者的解剖结果发现，他们并没有出现在细胞核而是在细胞质中凝聚——在胶质细胞中）

也就是我们必须发现所研究的目标蛋白会在病理状况下发生位置的改变？或者在病理状态下发生凝集？

（2）