• Home
  • Search Results
  • Nonclassical nuclear localization signals mediate nuclear import of CIRBP.

Nonclassical nuclear localization signals mediate nuclear import of CIRBP.

Proceedings of the National Academy of Sciences of the United States of America (2020-04-03)
Benjamin Bourgeois, Saskia Hutten, Benjamin Gottschalk, Mario Hofweber, Gesa Richter, Julia Sternat, Claudia Abou-Ajram, Christoph Göbl, Gerd Leitinger, Wolfgang F Graier, Dorothee Dormann, Tobias Madl

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.

Product Number
Product Description

Monoclonal Anti-Transportin 1 antibody produced in mouse, clone D45, purified immunoglobulin, buffered aqueous solution

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.