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Asymmetric Dimethylation of Ribosomal S6 Kinase 2 Regulates Its Cellular Localisation and Pro-Survival Function

Mahmoud I Khalil1,2, Heba M Ismail3,4, Ganna Panasyuk5,6

  • 1Molecular Biology Unit, Department of Zoology, Faculty of Science, Alexandria University, Alexandria 21568, Egypt.

International Journal of Molecular Sciences
|May 27, 2023
PubMed

Insights

Protein arginine methylation modifies Ribosomal S6 kinase 2 (S6K2), promoting its nuclear localization and pro-survival functions during starvation. This methylation is crucial for S6K2 activity in cancer progression.

Area of Science:

  • Cellular biology
  • Molecular oncology
  • Post-translational modifications

Background:

  • Ribosomal S6 kinases (S6Ks) regulate cell growth and survival, with dysregulation linked to cancer.
  • S6K1 is well-studied, but S6K2's role in cancer progression remains underexplored.
  • Protein arginine methylation is a key post-translational modification in cellular processes.

Purpose of the Study:

  • To investigate the post-translational modification of S6K2.
  • To elucidate the role of arginine methylation in S6K2 function and localization.
  • To explore the implications of S6K2 methylation in cancer biology.

Main Methods:

  • In vitro and in vivo association studies with protein arginine methyltransferases (PRMTs).
  • Analysis of S6K2 methylation at specific arginine residues (Arg-475 and Arg-477).
  • Cellular localization studies and assessment of survival effects under starvation conditions.

Main Results:

  • p54-S6K2 undergoes asymmetric dimethylation at Arg-475 and Arg-477.
  • S6K2 associates with PRMT1, PRMT3, and PRMT6, mediating this methylation.
  • Methylation drives nuclear localization of S6K2, essential for its pro-survival role during starvation-induced cell death.

Conclusions:

  • Arginine methylation is a novel regulatory mechanism for p54-S6K2 function.
  • This modification impacts S6K2's cellular localization and survival signaling.
  • S6K2 methylation may represent a significant factor in cancer progression, especially where arginine methylation is elevated.
Keywords:
AT-hookSCLCarginine methylationmethyltransferasesserine/threonine kinases

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