ArticleThe Journal of biological chemistry2017
The intrinsically disordered N-terminal domain of galectin-3 dynamically mediates multisite self-association of the protein through fuzzy interactions.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 87 citations in OpenAlex.
- Decoding Galectin-Glycan Recognition withJournal of the American Chemical Society · 2026Article
- Expression, Localization and Actions of Galectin-3: Implications in the Pathophysiology and Therapy of Cardiovascular Disease.International journal of molecular sciences · 2026Review
- Developing Galectin-3-Targeted Therapeutics in Diseases: Three Distinct Galectin-3 Segments for Targeting.Expert reviews in molecular medicine · 2026Review
- Evolution of intrinsically disordered regions in vertebrate galectins for phase separation.EMBO reports · 2026Article
- The Historiography of Galactose and Its Recognition by Galectins.Advances in experimental medicine and biology · 2026Review
- Article
- Galectin-3 directs mitophagy in response to Parkin-/proteasome-dependent rupture of mitochondrial outer membrane.Biology direct · 2025Article
- Missense mutations in intrinsically disordered protein regions link pathogenicity and phase separation.The Journal of biological chemistry · 2025Article
- Article
- Chimerolectins: Classification, structural architecture, and functional perspectives.Protein science : a publication of the Protein Society · 2025Review
- Sense, plug, and seal: proteins as both rapid responders and constitutive barriers supporting organelle compartmentalization.Molecular biology of the cell · 2025Review
- Galectin-3: Integrator of Signaling via Hexosamine Flux.Biomolecules · 2025Review
- Soybean Lectin Cross-Links Membranes by Binding Sulfatide in a Curvature-Dependent Manner.Journal of agricultural and food chemistry · 2025Article
- Galectin-3 in Cardiovascular Health: A Narrative Review Based on Life's Essential 8 and Life's Simple 7 Frameworks.Current issues in molecular biology · 2025Review
- PSTP: accurate residue-level phase separation prediction using protein conformational and language model embeddings.Briefings in bioinformatics · 2025Article
- Martini3-IDP: improved Martini 3 force field for disordered proteins.Nature communications · 2025Article
- Article
- Evolution and function of galectins inBBA advances · 2025Article
- Mammalian cell-based production of glycans, glycopeptides and glycomodules.Nature communications · 2024Article
- A Few Charged Residues in Galectin-3's Folded and Disordered Regions Regulate Phase Separation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
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Authors and funding
7 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Galectins are a family of lectins that bind β-galactosides through their conserved carbohydrate recognition domain (CRD) and can induce aggregation with glycoproteins or glycolipids on the cell surface and thereby regulate cell activation, migration, adhesion, and signaling. Galectin-3 has an intrinsically disordered N-terminal domain and a canonical CRD. Unlike the other 14 known galectins in mammalian cells, which have dimeric or tandem-repeated CRDs enabling multivalency for various functions, galectin-3 is monomeric, and its functional multivalency therefore is somewhat of a mystery. Here, we used NMR spectroscopy, mutagenesis, small-angle X-ray scattering, and computational modeling to study the self-association-related multivalency of galectin-3 at the residue-specific level. We show that the disordered N-terminal domain (residues ∼20-100) interacts with itself and with a part of the CRD not involved in carbohydrate recognition (β-strands 7-9; residues ∼200-220), forming a fuzzy complex via inter- and intramolecular interactions, mainly through hydrophobicity. These fuzzy interactions are characteristic of intrinsically disordered proteins to achieve liquid-liquid phase separation, and we demonstrated that galectin-3 can also undergo liquid-liquid phase separation. We propose that galectin-3 may achieve multivalency through this multisite self-association mechanism facilitated by fuzzy interactions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.