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Role of Protein Post-Translational Modifications in Cancer: Mechanisms and Therapeutic Opportunities

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

Deadline for manuscript submissions: 20 November 2025 | Viewed by 622

Special Issue Editors


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Guest Editor
Graduate Institute of Biomedical Science, China Medical University, Taichung 40402, Taiwan
Interests: the dysregulation of signal transduction; metabolic pathway in cancer progression; drug resistance
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Post-translational modifications (PTMs) represent a major biochemical mechanism for increasing the diversity of the proteome, allowing proteins to undergo functional changes that can be dynamically adjusted in response to both intracellular and extracellular signals. In cancer, PTMs such as phosphorylation, ubiquitination, acetylation, glycosylation, and methylation are not merely secondary modifications; rather, they influence virtually every hallmark of cancer. These and other modifications regulate key cellular functions such as cell cycle progression, apoptosis, DNA repair, immune responses, and metabolism. However, cancer cells frequently hijack PTMs, exploiting these mechanisms to promote uncontrolled growth, evade apoptosis, drive metastasis, and resist treatment.

The targeting of these aberrant PTM pathways presents a vast array of potential avenues for therapeutic intervention. One of the most well-known examples is the aberrant tyrosine kinase activity of the BCR-ABL fusion protein in chronic myeloid leukemia. Imatinib, a pioneering therapeutic agent that targets this hyperactive kinase and was specifically developed for this purpose, exemplifies how correcting PTM-driven dysregulation can result in effective cancer treatment, opening the door to a wide range of cancer treatments.

This Special Issue will collect the latest research on the pivotal roles of PTMs in the diverse stages and forms of cancer, with particular interest in mechanistic studies aimed at revealing how specific PTMs contribute to tumor initiation, progression, and metastasis. Furthermore, comprehensive reviews of current treatments targeting PTMs, which should examine the efficacy of existing therapies and highlight new therapeutic avenues, will be welcomed.

By collecting a broad spectrum of research, the aim is to provide a deeper understanding of the molecular mechanism controlled by PTMs in tumors and of how manipulating PTMs can revolutionize cancer treatment and improve patient outcomes.

You may choose our Joint Special Issue in Kinases and Phosphatases.

Dr. Mauro Salvi
Prof. Dr. Wei-Chien Huang
Dr. Josefa León
Guest Editors

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Keywords

  • phosphorylation
  • acetylation
  • methylation
  • sumoylation
  • ubiquitination
  • glycosylation
  • acylation
  • signal transduction
  • inhibitors

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Published Papers (1 paper)

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Research

13 pages, 3540 KB  
Communication
Comparative Efficacy of CK2 Inhibitors CX-4945 and SGC-CK2-2 on CK2 Signaling
by Francesca Noventa, Rina Venerando, Valentina Bosello Travain and Mauro Salvi
Int. J. Mol. Sci. 2025, 26(20), 10006; https://doi.org/10.3390/ijms262010006 - 14 Oct 2025
Viewed by 216
Abstract
The pleiotropic kinase CK2 plays a crucial role in numerous cellular processes and is frequently deregulated in human diseases. Specifically, elevated CK2 expression and/or activity have been observed in human cancers, thus rendering its inhibition a promising pharmacological strategy for treating malignancies. The [...] Read more.
The pleiotropic kinase CK2 plays a crucial role in numerous cellular processes and is frequently deregulated in human diseases. Specifically, elevated CK2 expression and/or activity have been observed in human cancers, thus rendering its inhibition a promising pharmacological strategy for treating malignancies. The most widely used CK2 inhibitor, CX-4945 (Silmitarsetib), was developed by Cylene Pharmaceuticals in 2010. It has been tested in clinical trials for various cancers and, more recently, as a potential therapy for COVID-19 patients. However, it has been demonstrated that CX-4945’s specificity is limited, as CX-4945 also inhibits other kinases beyond CK2. A recently developed derivative of CX-4945, SGC-CK2-2, has demonstrated enhanced specificity compared with CX-4945, albeit with reduced potency. In this study, we conducted a detailed analysis of the effects of SGC-CK2-2 in two cancer cell lines, comparing its efficacy with CX-4945 in inhibiting CK2 signaling and in cell death induction. The findings of this study demonstrate the differential sensitivity of CK2 phospho-substrates to these inhibitors, thus indicating that complete inhibition of a single phosphosite, such as S129 Akt, is insufficient to fully suppress CK2 signaling. Furthermore, the results suggest that partial CK2 inhibition with the suppression of the most sensitive phosphosites does not significantly impact cell viability, while a near-complete suppression of CK2 signaling affects cell viability and leads to cell death induction. Full article
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