scholarly journals Phase Separation of FUS Is Suppressed by Its Nuclear Import Receptor and Arginine Methylation

Cell ◽  
2018 ◽  
Vol 173 (3) ◽  
pp. 706-719.e13 ◽  
Author(s):  
Mario Hofweber ◽  
Saskia Hutten ◽  
Benjamin Bourgeois ◽  
Emil Spreitzer ◽  
Annika Niedner-Boblenz ◽  
...  
Keyword(s):  
Phase Separation ◽  
Nuclear Import ◽  
Arginine Methylation ◽  
Import Receptor

scholarly journals Nuclear Import Receptor Inhibits Phase Separation of FUS through Binding to Multiple Sites

Cell ◽  
2018 ◽  
Vol 173 (3) ◽  
pp. 693-705.e22 ◽  
Author(s):  
Takuya Yoshizawa ◽  
Rustam Ali ◽  
Jenny Jiou ◽  
Ho Yee Joyce Fung ◽  
Kathleen A. Burke ◽  
...  
Keyword(s):  
Phase Separation ◽  
Nuclear Import ◽  
Import Receptor

scholarly journals Arginine Methylation of the Nuclear Poly(A) Binding Protein Weakens the Interaction with Its Nuclear Import Receptor, Transportin

2011 ◽  
Vol 286 (38) ◽  
pp. 32986-32994 ◽  
Author(s):  
Katharina Fronz ◽  
Stefan Güttinger ◽  
Kerstin Burkert ◽  
Uwe Kühn ◽  
Nadine Stöhr ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Binding Protein ◽  
Arginine Methylation ◽  
Import Receptor

scholarly journals Targeting the Nuclear Import Receptor Kpnβ1 as an Anticancer Therapeutic

2016 ◽  
Vol 15 (4) ◽  
pp. 560-573 ◽  
Author(s):  
Pauline J. van der Watt ◽  
Alicia Chi ◽  
Tamara Stelma ◽  
Catherine Stowell ◽  
Erin Strydom ◽  
...  
Keyword(s):  
Nuclear Import ◽  
Import Receptor

scholarly journals Transportin Is a Major Nuclear Import Receptor for c-Fos

2006 ◽  
Vol 281 (9) ◽  
pp. 5492-5499 ◽  
Author(s):  
Marc Arnold ◽  
Annegret Nath ◽  
Daniel Wohlwend ◽  
Ralph H. Kehlenbach
Keyword(s):  
Nuclear Import ◽  
Import Receptor

scholarly journals The Requirement of H1 Histones for a Heterodimeric Nuclear Import Receptor

2002 ◽  
Vol 277 (36) ◽  
pp. 32480-32489 ◽  
Author(s):  
Marc Bäuerle ◽  
Detlef Doenecke ◽  
Werner Albig
Keyword(s):  
Nuclear Import ◽  
Import Receptor

scholarly journals Nonclassical nuclear localization signals mediate nuclear import of CIRBP

2020 ◽  
Vol 117 (15) ◽  
pp. 8503-8514 ◽  
Author(s):  
Benjamin Bourgeois ◽  
Saskia Hutten ◽  
Benjamin Gottschalk ◽  
Mario Hofweber ◽  
Gesa Richter ◽  
...  
Keyword(s):  
Phase Separation ◽  
Nuclear Localization ◽  
Nuclear Import ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Specific Interaction ◽  
Stress Granule ◽  
Rich Region ◽  
Nuclear Localization Signals ◽  
Cargo Proteins

The specific interaction of importins with nuclear localization signals (NLSs) of cargo proteins not only mediates nuclear import but also, prevents their aberrant phase separation and stress granule recruitment in the cytoplasm. The importin Transportin-1 (TNPO1) plays a key role in the (patho-)physiology of both processes. Here, we report that both TNPO1 and Transportin-3 (TNPO3) recognize two nonclassical NLSs within the cold-inducible RNA-binding protein (CIRBP). Our biophysical investigations show that TNPO1 recognizes an arginine-glycine(-glycine) (RG/RGG)–rich region, whereas TNPO3 recognizes a region rich in arginine-serine-tyrosine (RSY) residues. These interactions regulate nuclear localization, phase separation, and stress granule recruitment of CIRBP in cells. The presence of both RG/RGG and RSY regions in numerous other RNA-binding proteins suggests that the interaction of TNPO1 and TNPO3 with these nonclassical NLSs may regulate the formation of membraneless organelles and subcellular localization of numerous proteins.

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