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Kinase Signal Transduction 4.0
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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: closed (20 June 2024) | Viewed by 7614

Special Issue Editor

Prof. Dr. Atsushi Matsuzawa

E-Mail Website
Guest 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
Special Issues, Collections and Topics in MDPI journals

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

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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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Related Special Issues

Published Papers (4 papers)

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Research

14 pages, 2122 KiB  
Article
Gallic Acid Enhances the Efficacy of BCR::ABL1 Tyrosine Kinase Inhibitors in Chronic Myeloid Leukemia through Inhibition of Mitochondrial Respiration and Modulation of Oncogenic Signaling Pathways
by Wei Xiang, Colin Sng, Yi-Hui Lam, Ze-Hui Kok, Yeh-Ching Linn, Soek-Ying Neo, Yin-Yin Siew, Deepika Singh, Hwee-Ling Koh and Charles Chuah
Int. J. Mol. Sci. 2024, 25(14), 7958; https://doi.org/10.3390/ijms25147958 - 21 Jul 2024
Viewed by 1327
Abstract
While BCR::ABL1 tyrosine kinase inhibitors have transformed the treatment paradigm for chronic myeloid leukemia (CML), disease progression and treatment resistance due to BCR::ABL1-dependent and BCR::ABL1-independent mechanisms remain a therapeutic challenge. Natural compounds derived from plants have significantly contributed to cancer pharmacotherapy. This study [...] Read more.
While BCR::ABL1 tyrosine kinase inhibitors have transformed the treatment paradigm for chronic myeloid leukemia (CML), disease progression and treatment resistance due to BCR::ABL1-dependent and BCR::ABL1-independent mechanisms remain a therapeutic challenge. Natural compounds derived from plants have significantly contributed to cancer pharmacotherapy. This study investigated the efficacy of an active component of Leea indica, a local medicinal plant, in CML. Using high-performance liquid chromatography–electrospray ionization–mass spectrometry, a chemical constituent from L. indica extract was isolated and identified as gallic acid. Commercially obtained gallic acid was used as a chemical standard. Gallic acid from L. indica inhibited proliferation and induced apoptosis in CML cell lines, as did the chemical standard. Furthermore, gallic acid induced apoptosis and decreased the colony formation of primary CML CD34+ cells. The combination of isolated gallic acid or its chemical standard with BCR::ABL1 tyrosine kinase inhibitors resulted in a significantly greater inhibition of colony formation and cell growth compared to a single drug alone. Mechanistically, CML cells treated with gallic acid exhibited the disruption of multiple oncogenic pathways including ERK/MAPK, FLT3 and JAK/STAT, as well as impaired mitochondrial respiration. Rescue studies showed that gallic acid is significantly less effective in inducing apoptosis in mitochondrial respiration-deficient ρ0 cells compared to wildtype cells, suggesting that the action of gallic acid is largely through the inhibition of mitochondrial respiration. Our findings highlight the therapeutic potential of L. indica in CML and suggest that gallic acid may be a promising lead chemical constituent for further development for CML treatment. Full article
(This article belongs to the Special Issue Kinase Signal Transduction 4.0)
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17 pages, 2682 KiB  
Article
PKC Inhibition Improves Human Penile Vascular Function and the NO/cGMP Pathway in Diabetic Erectile Dysfunction: The Role of NADPH Oxidase
by Mariam El Assar, José M. La Fuente, Patricia Sosa, Argentina Fernández, Augusto J. Pepe-Cardoso, Juan I. Martínez-Salamanca, Leocadio Rodríguez-Mañas and Javier Angulo
Int. J. Mol. Sci. 2024, 25(6), 3111; https://doi.org/10.3390/ijms25063111 - 7 Mar 2024
Viewed by 1389
Abstract
Erectile dysfunction (ED) is a frequent and difficult-to-treat condition in diabetic men. Protein kinase C (PKC) is involved in diabetes-related vascular and cavernosal alterations. We aimed to evaluate the role of PKC in endothelial dysfunction and NO/cGMP impairment associated with diabetic ED in [...] Read more.
Erectile dysfunction (ED) is a frequent and difficult-to-treat condition in diabetic men. Protein kinase C (PKC) is involved in diabetes-related vascular and cavernosal alterations. We aimed to evaluate the role of PKC in endothelial dysfunction and NO/cGMP impairment associated with diabetic ED in the human corpus cavernosum (CC) and penile resistance arteries (PRAs) and the potential mechanisms involved. Functional responses were determined in the CC and PRAs in patients with non-diabetic ED and diabetic ED undergoing penile prosthesis insertion. PKC activator 12,13-phorbol-dibutyrate (PDBu) impaired endothelial relaxations and cGMP generation in response to acetylcholine in the CC from non-diabetic ED. PDBu also impaired responses to a PDE5 inhibitor, sildenafil, in non-diabetic ED patients. Conversely, a PKC inhibitor, GF109203X, improved endothelial, neurogenic, and PDE5-inhibitor-induced relaxations and cGMP generation only in the CC in diabetic ED patients. Endothelial and PDE5-inhibitor-induced vasodilations of PRAs were potentiated only in diabetes. Improvements in endothelial function in diabetes were also achieved with a specific inhibitor of the PKCβ2 isoform or an NADPH-oxidase inhibitor, apocynin, which prevented PDBu-induced impairment in non-diabetic patients. PKC inhibition counteracted NO/cGMP impairment and endothelial dysfunction in diabetes-related ED, potentially improving response to PDE5 inhibition. Full article
(This article belongs to the Special Issue Kinase Signal Transduction 4.0)
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21 pages, 3192 KiB  
Article
Akt Is Controlled by Bag5 through a Monoubiquitination to Polyubiquitination Switch
by Ismael Bracho-Valdés, Rodolfo Daniel Cervantes-Villagrana, Yarely Mabell Beltrán-Navarro, Adán Olguín-Olguín, Estanislao Escobar-Islas, Jorge Carretero-Ortega, J. Alberto Olivares-Reyes, Guadalupe Reyes-Cruz, J. Silvio Gutkind and José Vázquez-Prado
Int. J. Mol. Sci. 2023, 24(24), 17531; https://doi.org/10.3390/ijms242417531 - 15 Dec 2023
Viewed by 1818
Abstract
The serine-threonine kinase Akt plays a fundamental role in cell survival, metabolism, proliferation, and migration. To keep these essential processes under control, Akt activity and stability must be tightly regulated; otherwise, life-threatening conditions might prevail. Although it is well understood that phosphorylation regulates [...] Read more.
The serine-threonine kinase Akt plays a fundamental role in cell survival, metabolism, proliferation, and migration. To keep these essential processes under control, Akt activity and stability must be tightly regulated; otherwise, life-threatening conditions might prevail. Although it is well understood that phosphorylation regulates Akt activity, much remains to be known about how its stability is maintained. Here, we characterize BAG5, a chaperone regulator, as a novel Akt-interactor and substrate that attenuates Akt stability together with Hsp70. BAG5 switches monoubiquitination to polyubiquitination of Akt and increases its degradation caused by Hsp90 inhibition and Hsp70 overexpression. Akt interacts with BAG5 at the linker region that joins the first and second BAG domains and phosphorylates the first BAG domain. The Akt-BAG5 complex is formed in serum-starved conditions and dissociates in response to HGF, coincident with BAG5 phosphorylation. BAG5 knockdown attenuated Akt degradation and facilitated its activation, whereas the opposite effect was caused by BAG5 overexpression. Altogether, our results indicate that Akt stability and signaling are dynamically regulated by BAG5, depending on growth factor availability. Full article
(This article belongs to the Special Issue Kinase Signal Transduction 4.0)
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15 pages, 1857 KiB  
Article
Asymmetric Dimethylation of Ribosomal S6 Kinase 2 Regulates Its Cellular Localisation and Pro-Survival Function
by Mahmoud I. Khalil, Heba M. Ismail, Ganna Panasyuk, Anna Bdzhola, Valeriy Filonenko, Ivan Gout and Olivier E. Pardo
Int. J. Mol. Sci. 2023, 24(10), 8806; https://doi.org/10.3390/ijms24108806 - 15 May 2023
Cited by 1 | Viewed by 2142
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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