Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 117, Issue 15, Pages 8503-8514Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1918944117
Keywords
CIRBP; Transportin-1; Transportin-3; nuclear import; phase separation
Categories
Funding
- Austrian Science Foundation (FWF) [W 1226-B18]
- Nikon Austria
- Deutsche Forschungsgemeinschaft (DFG
- German Research Foundation) [DO1804/1-1, DO1804/3-1, DO1804/4-1, 390857198]
- Fritz Thyssen Foundation
- Paul Ehrlich Foundation
- Austrian Science Foundation [P28854, I3792, W1226]
- Austrian Research Promotion Agency (FFG) [864690, 870454]
- Integrative Metabolism Research Center Graz
- Austrian Infrastructure Program 2016/2017
- Styrian Government (Zukunftsfonds)
- BioTechMed-Graz
- Austrian Infrastructure Program 2013/2014
- Nikon Austria Inc.
- BioTechMed
- DFG [INST 86/1581-1 FUGG]
- Austrian Science Fund (FWF) [P28854] Funding Source: Austrian Science Fund (FWF)
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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 non-classical NLSs may regulate the formation of membraneless organelles and subcellular localization of numerous proteins.
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