Cancer Epigenetics, Post-Translational Modification, and Drug Discovery

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Cellular Biochemistry".

Deadline for manuscript submissions: 30 September 2025 | Viewed by 819

Special Issue Editor

Department of Pharmacology and Toxicology, Indiana University School of Medicine, 635 Barnhill Drive, Indianapolis, IN 46202, USA
Interests: multi-functional transcription factor nuclear factor κB (NF-κB); epigenetics; drug discovery; inflammation; cancer

Special Issue Information

Dear Colleagues,

This Special Issue aims to explore the intricate interplay between epigenetic regulation and molecular drivers in oncogenesis, with a particular focus on the role of multi-functional transcription factors such as NF-κB. NF-κB is a key orchestrator of inflammatory responses and oncogenic signaling, and it is intricately linked to epigenetic modifications that drive cancer progression and therapeutic resistance.

We invite contributions that delve into the complex networks connecting epigenetic reprogramming, chromatin remodeling, post-translational modification, and DNA methylation with the activation of NF-κB and other molecular pathways.

Submissions may include original research, comprehensive reviews, or perspectives.

Dr. Tao Lu
Guest Editor

Manuscript Submission Information

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Keywords

  • cancer
  • drug Discovery
  • epigenetics
  • inflammation
  • NF–κB

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Published Papers (2 papers)

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Research

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18 pages, 2486 KiB  
Article
The Unconventional Role of ABHD17A in Increasing the S-Palmitoylation and Antiviral Activity of IFITM1 by Downregulating ABHD16A
by Xuemeng Shi, Shuaiwu Chen, Mingyang Liu, Yali Fan, Xin Wen, Jingyi Wang, Xiaoling Li, Huimin Liu, Lin Mao, Li Yu, Yuxin Hu and Jun Xu
Biomolecules 2025, 15(7), 992; https://doi.org/10.3390/biom15070992 - 11 Jul 2025
Abstract
The broad-spectrum antiviral functions of interferon-inducible transmembrane 1 (IFITM1) rely on S-palmitoylation post-translational modification. α/β-hydrolase domain-containing 17A (ABHD17A) has been reported to be responsible for protein depalmitoylation over the past decade, but whether and how ABHD17A regulates the dynamic S-palmitoylation modification of IFITM1 [...] Read more.
The broad-spectrum antiviral functions of interferon-inducible transmembrane 1 (IFITM1) rely on S-palmitoylation post-translational modification. α/β-hydrolase domain-containing 17A (ABHD17A) has been reported to be responsible for protein depalmitoylation over the past decade, but whether and how ABHD17A regulates the dynamic S-palmitoylation modification of IFITM1 remains unknown. Here, we demonstrated that ABHD17A physically interacts with IFITM1 and increases the S-palmitoylation level of IFITM1. Sequence alignment revealed that ABHD17A lacked the DHHC motif, which is capable of catalyzing the S-palmitoylation modification. Thus, we screened multiple candidate palmitoylating and depalmitoylating enzymes that may contribute to ABHD17A-induced upregulation of IFITM1 S-palmitoylation. The recently discovered depalmitoylase ABHD16A was significantly downregulated by ABHD17A, which counteracted the palmitate-removing reactions of ABHD16A on IFITM1 and subsequently upregulated the S-palmitoylation level and antiviral activity of IFITM1. Our work therefore elucidated the unconventional role of depalmitoylase ABHD17A in elevating the S-palmitoylation modification, expanded the biological functions of ABHD17A in innate immunity, and provided potential targets for viral disease therapy. Full article
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Review

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24 pages, 1610 KiB  
Review
Lactylation: From Molecular Insights to Disease Relevance
by Yao Xu, Lu Zhang, Dong Shang and Hong Xiang
Biomolecules 2025, 15(6), 810; https://doi.org/10.3390/biom15060810 - 3 Jun 2025
Viewed by 653
Abstract
Lactylation, referring to the covalent coupling of the lactyl group with lysine residues, is a recently defined post-translational modification. It has been demonstrated that lactylation can alter protein transcription, thereby affecting the transmission of genetic information and ultimately exerting diverse effects on health [...] Read more.
Lactylation, referring to the covalent coupling of the lactyl group with lysine residues, is a recently defined post-translational modification. It has been demonstrated that lactylation can alter protein transcription, thereby affecting the transmission of genetic information and ultimately exerting diverse effects on health and diseases. Here, we review the existing literature and summarize the characteristics and mechanisms of lactylation on both histone and non-histone proteins. We hope to explore lactylation targets for different diseases, thus providing potential clues for new therapeutic strategies. Full article
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