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The Translation Process, Molecular Mechanism, and Recognition Methods of Post-Translational Modifications of Proteins

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

Deadline for manuscript submissions: closed (20 February 2026) | Viewed by 914

Special Issue Editor


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Guest Editor
Center for Informational Biology, School of Life Science and Technology, University of Electronic Science and Technology of China, Chengdu 610054, China
Interests: protein informatics; peptide sequence analysis; machine learning applications in biological macromolecular data; biomarker; protein post-translational modification site; systems biology; clinical data analysis; disease risk prediction; analysis and identification of DNA regulatory elements
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Special Issue Information

Dear Colleagues,

The Special Issue aims to explore the intricate relationship between protein synthesis and the subsequent modifications that influence protein function and cellular processes. Protein translation is a complex and highly regulated process that involves the decoding of genetic information into functional proteins. However, the functional diversity of proteins extends beyond their primary structure, with post-translational modifications (PTMs) playing a crucial role in regulating protein activity, stability, localization, and interactions. These modifications, including phosphorylation, acetylation, methylation, and ubiquitination, are key to cellular signaling, gene expression regulation, and the response to environmental stimuli. This issue will focus on recent advancements in understanding the molecular mechanisms underlying PTMs, how they influence protein function, and their contribution to cellular homeostasis and disease mechanisms. By bridging the translation process with PTM pathways, this Special Issue aims to provide insights into the dynamic regulation of proteins, opening new avenues for therapeutic interventions targeting protein modifications in various diseases, including cancer, neurodegenerative disorders, and metabolic diseases.

Prof. Dr. Hao Lin
Guest Editor

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Keywords

  • DNA replication, repair, and transcription
  • post-translational modifications
  • chromatin
  • acetylation, methylation, phosphorylation
  • ubiquitination and ubiquitin-like modifiers
  • histone modifications

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Published Papers (1 paper)

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Research

24 pages, 15199 KB  
Article
Phosphoproteomic Landscape of HDLBP: Insights into Function and Disease Associations
by Pathiyil Sajini Sekhar, Amal Fahma, Suhail Subair, Leona Dcunha, Althaf Mahin, Athira Perunally Gopalakrishnan, Rajesh Raju and Sowmya Soman
Int. J. Mol. Sci. 2026, 27(5), 2147; https://doi.org/10.3390/ijms27052147 - 25 Feb 2026
Viewed by 430
Abstract
High-density lipoprotein-binding protein (HDLBP), also called Vigilin, is a multifunctional RNA-binding protein with established roles in RNA transport and regulation, chromosome segregation, lipid homeostasis, and translational regulation. Frequently detected to be perturbed in phosphoproteome analysis, phosphorylation is indicated as a major mechanism in [...] Read more.
High-density lipoprotein-binding protein (HDLBP), also called Vigilin, is a multifunctional RNA-binding protein with established roles in RNA transport and regulation, chromosome segregation, lipid homeostasis, and translational regulation. Frequently detected to be perturbed in phosphoproteome analysis, phosphorylation is indicated as a major mechanism in the regulation of HDLBP functions; however, its phosphorylation landscape remains unexplored. We performed a meta-phosphoproteome analysis of HDLBP to map site-specific functional and regulatory roles of its two most frequently detected phosphosites, S31 and S944. Co-occurrence analysis across multiple datasets indicated that they can be phosphorylated together, suggesting potential co-ordinated regulation. Site-specific co-regulation analysis revealed distinct phospho-regulatory networks, with upstream kinases identified exclusively for S944. Functional enrichment of co-regulated protein phosphosites (CPPs) highlighted its role in RNA metabolism, chromosome organization, and nucleoplasmic transport, while functional annotation of site-specific phosphorylation of CPPs indicates its involvement in cell cycle regulation, apoptosis, and carcinogenesis. Additionally, the potential role of CPPs in the lipid homeostasis network was explored. Furthermore, the differential expression of HDLBP phosphosites across multiple cancers was observed using UALCAN, suggesting a potential role for phospho-regulation of HDLBP in tumor-associated pathways. Together, these findings provide the first integrated view of HDLBP phosphorylation and could serve as a valuable framework for future targeted studies to elucidate the mechanistic roles of site-specific HDLBP phosphorylation in cellular and pathophysiological processes. Full article
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