Mario Hofweber

TL;DR: It is shown that Transportin and arginine methylation have a crucial function beyond nuclear import-namely to suppress RGG/RG-driven phase separation and stress granule association of FUS.

TL;DR: Recent insights into how post-translational modifications of RBPs regulate phase separation and RNP granule dynamics are reviewed, in particular arginine (Arg)-methylation and phosphorylation.

TL;DR: It is shown that arginine-rich DPRs (poly-GR and poly-PR) bind directly to multiple importins and, in excess, promote their insolubility and condensation, and suggest that importins can decrease toxicity of arginin- rich DPRs by suppressing their pathological interactions.

TL;DR: It is reported that both TNPO1 and Transportin-3 (TNPO3) recognize two nonclassical NLSs within the cold-inducible RNA-binding protein (CIRBP), which regulate nuclear localization, phase separation, and stress granule recruitment of CIRBP in cells.

TL;DR: In this paper, the authors showed that FUS directly binds to different import receptors in vitro and in vivo, including transportin-3, importin-4 and importin β. Binding of these alternative import receptors required arginine residues within FUS-RG/RGG motifs.