Imperial College London

Dr Olivier E. Pardo

Faculty of MedicineDepartment of Surgery & Cancer

Reader in Cancer Cell Signalling
 
 
 
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Contact

 

+44 (0)20 7594 2814o.pardo Website CV

 
 
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Location

 

145ICTEM buildingHammersmith Campus

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Summary

 

Publications

Citation

BibTex format

@article{Khalil:2022:10.1101/2022.10.18.512681,
author = {Khalil, MI and Ismail, HM and Panasyuk, G and Gout, I and Pardo, OE},
doi = {10.1101/2022.10.18.512681},
title = {Asymmetric dimethylation of Ribosomal S6 Kinase 2 regulates its cellular localisation and pro-survival function},
url = {http://dx.doi.org/10.1101/2022.10.18.512681},
year = {2022}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - <jats:title>Abstract</jats:title><jats:p>Ribosomal S6 Kinases (S6Ks) are critical regulators of cell growth, homeostasis, and survival, with dysregulation of these kinases being associated with various malignancies. While S6K1 has been extensively studied, S6K2 has been neglected despite its reported involvement in cancer progression. Protein arginine methylation is a widespread post-translational modification regulating a plethora of biological responses in mammalian cells. Here we report that p54-S6K2 is asymmetrically dimethylated at Arg-475 and Arg-477, two conserved residues within the AT-hook motif of the S6K2 family and some AT-hook-containing proteins. We demonstrate that PRMT1, PRMT3, and PRMT6 bind to and methylate S6K2<jats:italic>in vitro</jats:italic>and<jats:italic>in vivo</jats:italic>. This methylation localises S6K2 to the nucleus where it rescues cells from starvation-induced cell death. Taken together, our findings highlight a novel mechanism regulating the biological function of p54-S6K2 that may be relevant to cancer where Arg-methylation is often found elevated.</jats:p>
AU - Khalil,MI
AU - Ismail,HM
AU - Panasyuk,G
AU - Gout,I
AU - Pardo,OE
DO - 10.1101/2022.10.18.512681
PY - 2022///
TI - Asymmetric dimethylation of Ribosomal S6 Kinase 2 regulates its cellular localisation and pro-survival function
UR - http://dx.doi.org/10.1101/2022.10.18.512681
ER -