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Post-translational modifications (PTMs) are vital regulators of protein function, influencing a myriad of cellular processes and disease mechanisms. Traditional experimental methods for PTM identification are both costly and labor-intensive, underlining the pressing need for efficient computational approaches. Early computational strategies predominantly relied on primary amino acid sequences and handcrafted features, which often lacked the contextual and structural understanding necessary for precise PTM site prediction. The emergence of transformer-based large language models (LLMs), particularly protein language models (pLMs), has revolutionized PTM prediction by producing context-aware embeddings that capture functional and structural intra-sequence dependencies. In this chapter, we provide a comprehensive review of recent advancements in leveraging LLMs (or, pLMs) for PTM site prediction, an important residue-level task in protein research. We identify emerging trends in the field, including the application of fine-tuning techniques, the integration of embeddings from multiple pLMs, and the incorporation of multiple modalities such as codon-aware embeddings, 3D structural data, and conventional representations. Additionally, we discuss tools that employ graph-based representations, the mamba architecture, and contrastive learning paradigms to further refine pLM-powered PTM site prediction models. We finally explore the interpretability and explainability aspects of the embeddings used in various tools. Despite the significant progress made, persistent limitations remain, and we outline these challenges while proposing directions for future research.
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http://dx.doi.org/10.1007/978-1-0716-4623-6_19 | DOI Listing |
J Am Soc Mass Spectrom
September 2025
School of Life Sciences, The Chinese University of Hong Kong, Sha Tin, N.T., Hong Kong, 999077.
Electrospray ionization (ESI)-mass spectrometry (MS) is a key platform for analyzing post-translationally modified proteins. With continuous advances in MS instruments and data analysis methods, top-down analysis of intact proteoforms has become highly feasible. To accurately quantify proteoforms with varying post-translational modifications (PTMs), the influence of PTMs on the ESI-MS detection efficiency must be considered.
View Article and Find Full Text PDFJ Biol Chem
September 2025
Department of Biological Sciences, The University of North Carolina at Charlotte, Charlotte, NC 28223.
Cdc37 is a kinase-specific co-chaperone that scaffolds protein kinase clients to the Hsp90 chaperone system. Although phosphorylation at residues S14 and S17 is known to regulate Cdc37 function, the broader role of phosphorylation across the protein remains unclear. To systematically investigate this, we created a "Cdc37 code collection," a set of 46 yeast strains expressing single phospho-site mutants of Cdc37, and performed phenotypic profiling across a wide panel of environmental and chemical stressors.
View Article and Find Full Text PDFFEBS J
September 2025
Faculty of Engineering and Natural Sciences, Sabancı University, Istanbul, Turkey.
The CRISPR/Cas9 system has revolutionized molecular biology and gene editing, yet key aspects of its regulation, especially within eukaryotic environments, remain enigmatic. In this Viewpoint article, I will speculate on and explore the provocative hypothesis that Cas9 may possess previously unrecognized effector-like functions when expressed in host cells, potentially shaped by host-mediated post-translational modifications (PTMs). Of particular interest is SUMOylation at lysine 848, a key residue for DNA binding within the catalytic site, raising the possibility that this modification is not incidental, but functionally significant and precisely regulated.
View Article and Find Full Text PDFJ Biol Chem
August 2025
Institute of Tumor Biology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany. Electronic address:
The developmental transcription factor grainyhead-like 2 (GRHL2) has been attributed both tumor-suppressive and pro-tumorigenic functions in a large variety of human cancers. Despite its fundamental role in cancer development and progression, mechanisms modulating expression or activity of GRHL2 in cancer cells still remain elusive. We identified several components of the SUMOylation machinery as candidate GRHL2 interactors using a yeast two-hybrid screening approach and a single major GRHL2 SUMOylation site at lysine residue 159.
View Article and Find Full Text PDFMethods Mol Biol
August 2025
Proteomics Program, Novo Nordisk Foundation Center for Protein Research, Department of Cellular and Molecular Medicine, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Small Ubiquitin-like Modifiers (SUMOs) are an important class of post-translational modification (PTM), modifying target proteins and thereby regulating virtually all nuclear processes. Various proteomics methods exist for profiling SUMO target proteins or SUMOylated lysine residues in a systemic manner, typically based on purification of SUMO followed by mass spectrometry (MS), with most approaches relying on ectopically expressed or mutant SUMO. However, to properly understand the role of SUMO in the context of health and disease, it is necessary to study native and endogenous SUMOylation, rather than relying on genetically engineered systems.
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