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Protein Kinase in Disease, 2nd Edition
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Protein Kinase in Disease, 2nd Edition

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: 20 February 2026 | Viewed by 1759

Special Issue Editor

Dr. Manae Suzuki Kurokawa

E-Mail Website
Guest Editor
Disease Biomarker Analysis and Molecular Regulation, Graduate School of Medicine, St Marianna University, Miyamae Ku, 2-16-1 Sugao, Kawasaki 2168511, Kanagawa, Japan
Interests: protein kinases; phosphorylation; cancers; inflammatory diseases; protein kinase inhibitors; anticancer drugs
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Protein kinases are enzymes that transfer ATP-γ-phosphate to the hydroxy groups of serine, threonine, and tyrosine residues of substrate proteins. Through phosphorylation of substrate proteins, protein kinases regulate their biological activity, cellular location, and interaction with other proteins to conduct signal transduction for cell proliferation, differentiation, and metabolism. The fine tuning of protein phosphorylation is crucial for orchestrating protein networks, which are essential for vital functions.  A total of 518 putative protein kinases have been identified in the human genome. They are divided into serine/threonine kinases and tyrosine kinases. The former group is further divided into seven subgroups (AGC, CAMK, CK1, CMGC, RGC, STE, and TKL), while the latter group is divided into two subgroups (receptor type and non-receptor type). Abnormality of protein kinases due to chromosomal mutation, translocation and deletion, aberrant splicing, and protein overexpression and loss of function is involved in developmental anomalies and various diseases such as cancers, inflammatory diseases, and metabolic disorders (e.g., diabetes mellitus). It is also related to the occurrence of cardiovascular diseases, neuronal degeneration, immune dysregulation, renal diseases, and sense organ disorders. Therapeutic strategies targeting these protein kinases are being explored. This has already led to the discovery of more than 40 protein kinase inhibitors as anticancer drugs. Further analysis of protein kinases associated with diseases and the development of novel protein kinase inhibitors may help to overcome intractable diseases.

Dr. Manae Suzuki Kurokawa
Guest Editor

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Keywords

  • protein kinases
  • phosphorylation
  • cancers
  • inflammatory diseases
  • protein kinase inhibitors
  • anticancer drugs

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Related Special Issue

Published Papers (2 papers)

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Research

17 pages, 1784 KB  
Article
Signaling via C-C Chemokine Ligand 19 and Extracellular Regulated Kinase 5 in T Cells Limits the Humoral Adaptive Immune Response in Mice
by Jaisel A. Cervantes, T. Paul Welch, Brian Kaiser, Charles A. Bill, Angel Torres, Gareth L. Bill, Colin A. Bill and Charlotte M. Vines
Int. J. Mol. Sci. 2025, 26(19), 9744; https://doi.org/10.3390/ijms26199744 - 7 Oct 2025
Viewed by 545
Abstract
Misregulation of C-C chemokine receptor 7 (CCR7) has been linked to multiple autoimmune diseases including systemic lupus erythematosus, multiple sclerosis, and ankylosing spondylitis. As a G-protein-coupled receptor, located on the cell membrane, CCR7 can be targeted by inhibiting one of its two ligands, [...] Read more.
Misregulation of C-C chemokine receptor 7 (CCR7) has been linked to multiple autoimmune diseases including systemic lupus erythematosus, multiple sclerosis, and ankylosing spondylitis. As a G-protein-coupled receptor, located on the cell membrane, CCR7 can be targeted by inhibiting one of its two ligands, C-C chemokine ligand 19 (CCL19), to regulate its function. In this study, we examined signaling events downstream of CCL19 binding that provide a mechanism for regulation of the immune response. We used a CCR7 antagonist, CCL198-83, in immune studies in vivo, as a platform for a pharmaceutical to define the molecular events that are involved in regulating the humoral adaptive immune response. We found that in the presence of a T-cell-dependent antigen, C57BL/6 mice treated during antigen exposure with CCL198-83 generated significantly higher levels of IgG1, the dominant isotype in extracellular bacterial infections that can activate complement, and IgG2c, the dominant isotype during viral and intracellular bacterial infections. Inhibiting ERK5 signaling downstream of CCR7 activation by CCL19, or disruption of CCL19 expression in CCL19−/− mice, also resulted in higher levels of IgG1 when compared to control mice. Differences in levels of IL-4 or other cytokines or lymphocyte types between wild-type and ERK5-deficient T cells did not account for antibody levels. Since pertussis-toxin-induced inhibition of lymphocyte chemotaxis is linked to elevated levels of IgG, we examined the effect of ERK5 on chemotaxis to CCR7 ligand CCL19. We found that disruption of ERK5 in T cells, or global disruption of CCL19 or CCR7, inhibited chemotaxis of T cells to CCL19, a mechanism that enhances sensitization during the exposure to an immunogen. Since CCR7 and its ligands have been linked to autoimmunity, these studies may provide insight into mechanisms that can be targeted to control autoimmune responses. Full article
(This article belongs to the Special Issue Protein Kinase in Disease, 2nd Edition)
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12 pages, 4644 KB  
Article
Molecular Dynamics Simulations of the SPRED2Leu100Pro EVH-1 Domain Complexed with the GAP-Related Domain of Neurofibromin
by Martina Terrusa, Elisa Sangiovanni, Marialetizia Motta, Marco Tartaglia, Ingrid Guarnetti Prandi and Giovanni Chillemi
Int. J. Mol. Sci. 2025, 26(9), 4342; https://doi.org/10.3390/ijms26094342 - 2 May 2025
Cited by 1 | Viewed by 723
Abstract
The homozygous Leu100Pro amino acid substitution in SPRED2, a protein negatively controlling RAS function, has recently been identified to be causally linked to a recessive form of Noonan syndrome. The amino acid substitution was documented to affect protein stability and cause a decreased [...] Read more.
The homozygous Leu100Pro amino acid substitution in SPRED2, a protein negatively controlling RAS function, has recently been identified to be causally linked to a recessive form of Noonan syndrome. The amino acid substitution was documented to affect protein stability and cause a decreased and/or less stable interaction with neurofibromin, a RAS-specific GTPase activating protein negatively regulating RAS function. To further investigate the structural and functional impact of Leu100Pro, we structurally characterized the consequences of this change on the interaction of SPRED2 with neurofibromin, by 1 µn-long molecular dynamics (MD) simulations. Our analyses failed in identifying local perturbations predicted to disrupt or dramatically affect SPRED2 binding to neurofibromin, though a rearrangement of their interaction was observed. On the other hand, MD simulations also identified long-range structural rearrangements of the SPRED2 EVH-1 domain, which might be relevant for an aberrant folding of the mutant driving the previously documented accelerated degradation. Overall, the performed MD simulations suggest the occurrence of multiple intramolecular and intermolecular structural perturbations driven by the Leu100Pro change that likely contribute to its LoF behavior. Full article
(This article belongs to the Special Issue Protein Kinase in Disease, 2nd Edition)
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