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Special Issue "Kinase Signal Transduction 4.0"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 31 December 2023 | Viewed by 1137

Special Issue Editor

Laboratory of Health Chemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba, Aramaki, Aoba-ku, Sendai, Miyagi 980-8578, Japan
Interests: kinase signal transduction; MAP kinase signaling; stress response; ubiquitination; post-translational modifications; redox signaling; cell death; innate immunity; inflammasome; cancer; drug toxicity
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Special Issue Information

Dear Colleagues,

Protein kinases phosphorylate a wide variety of substrates, which changes their conformation, activity, stability, intracellular localization, and affinity to other molecules. Therefore, protein kinases are critical for various biological functions and cellular processes, such as signal transduction, transcription, protein degradation, vesicle transport, cell growth and death, stress response, immunoregulation, and metabolism. Various types of protein kinases and their regulators have been identified and play a pivotal role in the determination of cell fate. The dysregulation of the protein kinase signal transduction leads to various diseases, including cancer, inflammation, autoimmune disorder, neurodegeneration, heart failure, ischemia, and diabetes, indicating that protein kinases and their regulators are important therapeutic targets for these diseases. Thus, understanding how protein kinases respond to stimuli and regulate cellular functions is crucial both biologically and clinically. This Special Issue, entitled “Kinase Signal Transduction”, welcomes contributions in all areas of recent research associated with novel physiological and pathological functions and regulatory mechanisms of protein kinases, as shown above.

Prof. Dr. Atsushi Matsuzawa
Guest Editor

Manuscript Submission Information

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Keywords

  • protein kinases
  • phosphorylation signal
  • transduction signaling
  • pathway cellular response
  • MAP kinase cascade protein
  • phosphatase signaling
  • complex signalosome signaling system

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Published Papers (1 paper)

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Research

Article
Asymmetric Dimethylation of Ribosomal S6 Kinase 2 Regulates Its Cellular Localisation and Pro-Survival Function
Int. J. Mol. Sci. 2023, 24(10), 8806; https://doi.org/10.3390/ijms24108806 - 15 May 2023
Viewed by 959
Abstract
Ribosomal S6 kinases (S6Ks) are critical regulators of cell growth, homeostasis, and survival, with dysregulation of these kinases found to be associated with various malignancies. While S6K1 has been extensively studied, S6K2 has been neglected despite its clear involvement in cancer progression. Protein [...] Read more.
Ribosomal S6 kinases (S6Ks) are critical regulators of cell growth, homeostasis, and survival, with dysregulation of these kinases found to be associated with various malignancies. While S6K1 has been extensively studied, S6K2 has been neglected despite its clear involvement in cancer progression. Protein arginine methylation is a widespread post-translational modification regulating many biological processes in mammalian cells. Here, we report that p54-S6K2 is asymmetrically dimethylated at Arg-475 and Arg-477, two residues conserved amongst mammalian S6K2s and several AT-hook-containing proteins. We demonstrate that this methylation event results from the association of S6K2 with the methyltransferases PRMT1, PRMT3, and PRMT6 in vitro and in vivo and leads to nuclear the localisation of S6K2 that is essential to the pro-survival effects of this kinase to starvation-induced cell death. Taken together, our findings highlight a novel post-translational modification regulating the function of p54-S6K2 that may be particularly relevant to cancer progression where general Arg-methylation is often elevated. Full article
(This article belongs to the Special Issue Kinase Signal Transduction 4.0)
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