Search bioRxiv⌕ Search

bioRxiv · 10.1101/2025.06.04.657817

A simple workflow to identify novel Small Linear Motif (SLiM)-mediated interactions with AlphaFold

Abstract

Short linear motifs (SLiMs) are highly compact interaction modules embedded within disordered protein regions and are increasingly recognized for their central role in maintaining cellular homeostasis. Due to their small size, degeneracy and transient binding, SLiMs remain difficult to detect both experimentally and computationally. Here, we show that AlphaFold, used via ColabFold, offers a practical and accessible alternative for in-silico SLiM discovery. Unlike previous studies focused on structural accuracy, we evaluated AlphaFolds capacity to reveal SLiMs independently of model quality. To this end, we benchmarked several scoring metrics and showed that AlphaFold2 combined with MiniPAE yields the best performance, outperforming AlphaFold3 in this context. Building on these findings, we also provide a streamlined and cost-effective workflow for SLiM prediction requiring no installation or local computation. To overcome challenges associated with SLiM validation, we also introduce a highly sensitive detection method based on proximity labeling in living cells. This workflow was used to predict the occurrence of SLiMs that mediate binding to ribosomal protein S6 kinase A3 (RPS6KA3 or RSK2). By leveraging Colabfold and MiniPAE available through Colab notebooks, our approach provides a scalable and widely accessible strategy for identifying functional SLiMs in proteins of interest. MiniPAE can be accessed at https://github.com/martinovein/MiniPAE Short descriptionMartin Veinstein is a PhD student in Biomedical Sciences at the de Duve Institute, UCLouvain, Belgium. He specializes in Small Linear Motifs (SLiMs) in the context of host-virus interactions and has developed strong expertise in bioinformatics, structural biology, and predictive modeling. Victor J is a unfergradiate student at the ECAM Brussels Engineering School, Haute Ecole "ICHEC-ECAM-ISFSC", Brussels, Belgium. His activities span form September to November 2023. B.I. Iorga is a CNRS Research Director at the Institut de Chimie des Substances Naturelles in Gif-sur-Yvette, France. His research focuses among others on methodological developments in molecular modeling and the in-silico prediction of antibiotic resistance using machine learning and deep learning approaches. Raphael Helaers is a Senior Investigator and leads bioinformatics infrastructure at the de Duve Institute, UCLouvain, Belgium. He has developed strong expertise in next-generation sequencing and software development, along with a deep interest in biology, genetics, and evolution. Thomas Michiels is a Full Professor and researcher at the de Duve Institute, UCLouvain, Belgium. His research focuses on virus-mediated subversion of the innate immune response. Frederic Sorgeloos is an adjunct Professor at the INRS, Laval, Canada. He currently focuses on the subversion of cellular homeostasis through small linear peptides encoded by viral and bacterial pathogens. Short abstractVarious AlphaFold2/3 scoring metrics were systematically benchmarked for their ability to detect Small Linear Motifs (SLiMs) Based on this evaluation, a user-friendly and cost-effective in-silico workflow is proposed to identify novel SLiMs-targeting proteins The utility of this workflow is demonstrated through the prediction of previously uncharacterized SLiMs interacting with RSK kinases. A sensitive in-vitro assay is proposed to streamline the validation of low-affinity SLiM-target interactions. Together, our workflow and associated validation assay offer an integrated pipeline for the discovery and validation of SLiM-mediated protein-protein interactions.

Source connections

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Veinstein, M., Janssens, V., Iorga, B. I., Helaers, R., Michiels, T., Sorgeloos, F.. 2025-06-08. A simple workflow to identify novel Small Linear Motif (SLiM)-mediated interactions with AlphaFold. https://doi.org/10.1101/2025.06.04.657817

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Comparative functional genomics reveals distributed SERPINE1 like characteristics among Drosophila serpins

Serpins (serine protease inhibitors) regulate proteolytic activity through a suicide-substrate inhibitory mechanism, whereby the serpin covalently traps and inactivates their target protease. Serpins are broadly conserved across eukaryotes, but the evolutionary and functional relationships between human SERPINE1, and Drosophila Serpins in incompletely defined. To identify candidate Drosophila functional analogs of SERPINE1/PAI-1, a multi-omics framework was applied to thoroughly compare the serpins across species. The multi-level analysis integrated orthology prediction, protein sequence and structural characterization, phylogenetic reconstruction, bulk tissue transcriptomics, single-cell transcriptomics, and aging-associated expression analysis. Candidate serpins (Spn42Da, Spn42Db, Spn42Dc, Spn42Dd, Spn28B, and Spn28F) were evaluated using DIOPT, AlphaFold/ChimeraX structural comparisons, reactive center loop analyses, phylogenetic distances, GTEx, Human Protein Atlas, FlyAtlas2, Fly Cell Atlas, and Aging Fly Cell Atlas datasets. Comparative analyses demonstrated full-length sequence and reactive center loop (RCL) divergence despite preservation of the canonical serpin fold. Tissue, cell-type, and age-associated expression analysis revealed distinct candidate-specific patterns. Spn42Dd comparisons uncovered similarities to human SERPINE1 in sequence/structural and broad expression but did not represent the strongest overall cross-species expression correlations. Spn42Da and Spn42Db received the highest cross species integrated support. Quality check of the ranking confirmed that Spn42Da and Spn42Db were stable top candidates across orthology, sequence alignment, and expression domains. The multi-domain analysis was unable to identify a single definitive Drosophila serpin as the closest counterpart to human SERPINE1, indicating that cross-species similarity is distributed across multiple candidate serpins. This study therefore provides a quantitative method for prioritizing potential evolutionary and functional analogs across highly divergent species.

bioinformatics↗

CellChat Hotspot: A Targeted Approach to Cell Cell Communication Analysis With Spatial transcriptomics Validation.

Abstract. In recent years, single cell RNA sequencing (scRNA seq) has enabled the investigation of intercellular communication through Cell Cell Communication (CCC) tools such as CellChat. Despite their potential, these approaches remain challenging to interpret, particularly when global analyses generate complex interaction networks that may include biologically irrelevant signals. To address this limitation, we developed a framework termed CellChat Hotspot, designed to improve the biological interpretability of inferred communication networks. This approach integrates gene set enrichment analysis with a context driven filtering strategy, selecting both genes and cells based on their functional relevance prior to communication inference. Applied to stage II colon cancer data, CellChat Hotspot enabled the identification of condition-specific interaction patterns associated with recurrence. Non recurrent patients showed enrichment of immune related processes, whereas recurrent cases were characterized by pathways associated with invasion and metastasis. Notably, a loss of interaction in the HSPG pathway between CALB1+ and stromal cells was observed in recurrent patients, suggesting a potential disruption of cell matrix adhesion mechanisms. To verify the reliability of this finding, we applied the framework to spatial transcriptomics data, which confirmed the presence of the HSPG2 DAG1 interaction in non-recurrent tumors and its near absence in recurrent ones. Overall, this framework provides a biologically guided strategy for studying intercellular communication in complex systems such as the tumor microenvironment.

bioinformatics↗

DiffTernary: a Diffusion Model for Molecular Glue Ternary Complex Docking

Molecular glues (MGs) modulate protein function by inducing or stabilizing protein interactions. However, accurately modeling MG ternary complexes remains challenging. Here, we present DiffTernary, a diffusion-based docking method for the joint prediction of relative protein arrangement and MG binding pose. We introduce Ternary-PDB, a dataset of 76,702 experimentally determined ternary complexes curated from the Protein Data Bank using structural filters and a release cutoff aligned with AlphaFold 3 (AF3). When trained on this dataset, DiffTernary achieved acceptable protein-protein interaction (PPI) predictions (DockQ > 0.23) for 50.0% of MGBench complexes with a single prediction, compared with 51.1% for AF3. In comparisons with AF3, OpenFold3, ESMFold2, Protenix-v1 and Protenix-v2, DiffTernary ranked second with a best-of-25 PPI prediction success rate of 78.4%, behind ESMFold2 (90.9%) and ahead of AF3 (72.7%). A separate DiffTernary model trained on TernaryDB achieved a mean DockQ of 0.306 on the 94 complexes in the TernaryDB MGD test set with a single prediction, compared with 0.228 for DeepTernary. Confidence-based selection among 40 samples yielded acceptable PPI predictions for 41.5% of complexes, compared with 30.9% for DeepTernary. An E2Former variant increased training and sampling throughput 6.90-fold and 4.37-fold, respectively, under the evaluated configurations. Together, DiffTernary and Ternary-PDB provide an efficient docking approach for MG complex prediction and a valuable structural resource for MG discovery and design.

bioinformatics↗