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Accurate SUMOylation site prediction is crucial for deciphering gene regulation and disease mechanisms. However, distinguishing SUMO1 and SUMO2 modifications remains a major challenge due to their structural similarities. Conventional prediction models often struggle to differentiate between these paralogues, limiting their applicability in biological research. To address this, we introduce SUMO-LMNet, a deep learning-based framework for the precise prediction of SUMO1 and SUMO2 sites. Unlike previous models, SUMO-LMNet integrates a lossless mapping strategy and deep learning architectures to enhance both prediction accuracy and interpretability. Our model extracts high-dimensional features from sequences and transforms them into two-dimensional feature maps, enabling convolutional neural networks (CNNs) to effectively capture both local and global dependencies within the data. By leveraging a Lossless Mapping Network (LM-Net), this approach preserves the original feature space, ensuring that feature integrity is retained without loss of spatial information. While Grad-CAM highlights key features in individual predictions, it lacks consistency across samples and does not provide a dataset-wide evaluation of feature importance. To address this, we introduce Combined Heatmap Feature Analysis (CHFA), which systematically aggregates feature importance across multiple samples, providing a more reliable and interpretable dataset-wide assessment. Experimental results reveal distinct feature dependencies between SUMO1 and SUMO2, underscoring the necessity of paralogue-specific predictive models. Through a systematic comparison of multiple neural network architectures, we demonstrate that our model achieves over 80 % accuracy in distinguishing SUMO1 and SUMO2 modification sites. By prioritizing candidate sites for further study, our model aids experimental design and accelerates the discovery of biologically relevant SUMOylation targets. SUMO-LMNet is publicly available at https://predictor.isu.edu.tw/sumo-lmnet.
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http://dx.doi.org/10.1016/j.csbj.2025.03.005 | DOI Listing |
Methods Mol Biol
August 2025
The University of Texas at El Paso (UTEP), El Paso, TX, USA.
We present an innovative method to specifically decrease SUMO2 SUMOylation by using a set of vivo-morpholinos inducing an alternative splicing event that produces a mRNA coding for SUMO2alpha, a non-conjugatable form of SUMO2. This method, also applicable to target SUMO1 and SUMO3, provides an alternative approach to assess the function of the various SUMO paralogs in different cells and the SUMO paralog preference of any given SUMO target.
View Article and Find Full Text PDFMethods Mol Biol
August 2025
Andalusian Center for Molecular Biology and Regenerative Medicine (CABIMER), Universidad de Sevilla-CSIC-Universidad Pablo de Olavide, Sevilla, Spain.
SUMOylation is a dynamic and reversible post-translational modification that occurs on acceptor lysines of substrate proteins. SUMO is conjugated via a dedicated enzymatic cascade of E1-E2-E3 enzymes, where the E3 confers substrate specificity. More than 6500 SUMO2/3 target proteins have been identified by mass spectrometry-based proteomics with important regulatory roles, predominantly in nuclear processes.
View Article and Find Full Text PDFMethods Mol Biol
August 2025
SUMO Biology Lab, School of Molecular and Cellular Biology, Astbury Centre for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, West Yorkshire, UK.
Tools to detect endogenous SUMOylation are critical for capturing and analyzing SUMOylation dynamics. Proteome-wide analysis of SUMOylation has provided invaluable insight into our understanding of global patterns of SUMOylation under various developmental and stressor conditions. Experimental validation of SUMOylation is still essential for a detailed mechanistic understanding of SUMOylation of individual proteins.
View Article and Find Full Text PDFEMBO J
August 2025
Birmingham Centre for Genome Biology and Department of Cancer and Genomic Sciences, School of Medical Sciences, College of Medicine and Health, University of Birmingham, Birmingham, B15 2TT, UK.
Mammalian cells express three conjugatable SUMO variants: SUMO1 and the closely related SUMO2 and SUMO3 (together referred to as SUMO2/3). While some substrates are modified by both, others show a clear preference, though the basis for this selectivity remains unclear. Here, we examine a modification of the catalytic component of the human SUMO activation enzyme, SAE2.
View Article and Find Full Text PDFCell Death Dis
July 2025
Centro de Investigación en Medicina Molecular (CIMUS), Universidade de Santiago de Compostela, Instituto de Investigaciones Sanitarias (IDIS), Santiago de Compostela, Spain.
p14ARF is a lysine-less tumor suppressor that enhances SUMOylation of its interactors. Although p14ARF is known to interact with the E2 SUMO conjugating enzyme UBC9, the link between ARF and SUMOylation is poorly understood and the potential impact of SUMOylation on p14ARF is unknown. Here we show that SUMO2 conjugates to the N-terminus of p14ARF and stabilizes it.
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