ArticleThe Biochemical journal2021
Kinetics of the multitasking high-affinity Win binding site of WDR5 in restricted and unrestricted conditions.
Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 14 citations in OpenAlex.
- Comparative Real-Time Kinetics of Ligand-Receptor Interactions Using Immobilization-Based Sensing Readouts.Analytical chemistry · 2026Article
- A Site-Specific Self-Association of a Protein Hub Drives Its Phase Separation.ACS chemical biology · 2026Article
- Real-Time Binding Kinetics of Membrane Protein-Protein Interactions in a Membraneless Setting.Analytical chemistry · 2025Article
- Hub Occupancy by Competitively Interacting Proteins Obeys a Simple Queuing Law.The journal of physical chemistry. B · 2025Article
- Single-Molecule Observation of Competitive Protein-Protein Interactions Utilizing a Nanopore.ACS nano · 2025Article
- O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): Potential mechanistic targets revealed by evaluating the OGT interactome.The Journal of biological chemistry · 2024Review
- Real-Time Measurement of a Weak Interaction of a Transcription Factor Motif with a Protein Hub at Single-Molecule Precision.ACS nano · 2024Article
- Overlapping characteristics of weak interactions of two transcriptional regulators with WDR5.International journal of biological macromolecules · 2024Article
- Article
- A generalizable nanopore sensor for highly specific protein detection at single-molecule precision.Nature communications · 2023Article
- Convergent Alterations of a Protein Hub Produce Divergent Effects within a Binding Site.ACS chemical biology · 2022Article
- Interplay of Affinity and Surface Tethering in Protein Recognition.The journal of physical chemistry letters · 2022Article
- Disentangling the recognition complexity of a protein hub using a nanopore.Nature communications · 2022Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
Recent advances in quantitative proteomics show that WD40 proteins play a pivotal role in numerous cellular networks. Yet, they have been fairly unexplored and their physical associations with other proteins are ambiguous. A quantitative understanding of these interactions has wide-ranging significance. WD40 repeat protein 5 (WDR5) interacts with all members of human SET1/MLL methyltransferases, which regulate methylation of the histone 3 lysine 4 (H3K4). Here, using real-time binding measurements in a high-throughput setting, we identified the kinetic fingerprint of transient associations between WDR5 and 14-residue WDR5 interaction (Win) motif peptides of each SET1 protein (SET1Win). Our results reveal that the high-affinity WDR5-SET1Win interactions feature slow association kinetics. This finding is likely due to the requirement of SET1Win to insert into the narrow WDR5 cavity, also named the Win binding site. Furthermore, our explorations indicate fairly slow dissociation kinetics. This conclusion is in accordance with the primary role of WDR5 in maintaining the functional integrity of a large multisubunit complex, which regulates the histone methylation. Because the Win binding site is considered a key therapeutic target, the immediate outcomes of this study could form the basis for accelerated developments in medical biotechnology.
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Registered trials
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