The glycine arginine-rich domain of the RNA-binding protein nucleolin regulates its subcellular localization
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00545891" target="_blank" >RIV/61388963:_____/21:00545891 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.15252/embj.2020107158" target="_blank" >https://doi.org/10.15252/embj.2020107158</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.15252/embj.2020107158" target="_blank" >10.15252/embj.2020107158</a>
Alternative languages
Result language
angličtina
Original language name
The glycine arginine-rich domain of the RNA-binding protein nucleolin regulates its subcellular localization
Original language description
Nucleolin is a multifunctional RNA Binding Protein (RBP) with diverse subcellular localizations, including the nucleolus in all eukaryotic cells, the plasma membrane in tumor cells, and the axon in neurons. Here we show that the glycine arginine rich (GAR) domain of nucleolin drives subcellular localization via protein-protein interactions with a kinesin light chain. In addition, GAR sequences mediate plasma membrane interactions of nucleolin. Both these modalities are in addition to the already reported involvement of the GAR domain in liquid-liquid phase separation in the nucleolus. Nucleolin transport to axons requires the GAR domain, and heterozygous GAR deletion mice reveal reduced axonal localization of nucleolin cargo mRNAs and enhanced sensory neuron growth. Thus, the GAR domain governs axonal transport of a growth controlling RNA-RBP complex in neurons, and is a versatile localization determinant for different subcellular compartments. Localization determination by GAR domains may explain why GAR mutants in diverse RBPs are associated with neurodegenerative disease.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
<a href="/en/project/GX19-26854X" target="_blank" >GX19-26854X: Concert of lipids, ions, and proteins in cell membrane dynamics and function</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
EMBO Journal
ISSN
0261-4189
e-ISSN
1460-2075
Volume of the periodical
40
Issue of the periodical within the volume
20
Country of publishing house
GB - UNITED KINGDOM
Number of pages
22
Pages from-to
e107158
UT code for WoS article
000695159300001
EID of the result in the Scopus database
2-s2.0-85114717476