Medizinische Universität Graz Austria/Österreich - Forschungsportal - Medical University of Graz
Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Bourgeois, B; Hutten, S; Gottschalk, B; Hofweber, M; Richter, G; Sternat, J; Abou-Ajram, C; Göbl, C; Leitinger, G; Graier, WF; Dormann, D; Madl, T.
Nonclassical nuclear localization signals mediate nuclear import of CIRBP.
Proc Natl Acad Sci U S A. 2020; 117(15): 8503-8514.
Doi: 10.1073/pnas.1918944117
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- Führende Autor*innen der Med Uni Graz
- Bourgeois Benjamin Michel Rene
- Madl Tobias
- Co-Autor*innen der Med Uni Graz
- Gottschalk Benjamin
- Graier Wolfgang
- Leitinger Gerd
- Richter Gesa Lucia
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- Abstract:
- 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. Copyright © 2020 the Author(s). Published by PNAS.
- Find related publications in this database (Keywords)
- CIRBP
- Transportin-1
- Transportin-3
- nuclear import
- phase separation