ReviewFrontiers in molecular biosciences2019
Analysis of α-Dystroglycan/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains.
Review in Frontiers in molecular biosciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Roles and therapeutic prospects of the laminin family in disorders of the nervous system.Journal of translational medicine · 2026Review
- Inactivation of calcium Ion signaling in neuronal SK-N-SH cells with development of resistance to a designer drug α-pyrrolidinooctanophenone.Forensic toxicology · 2026Article
- Review
- Glycosaminoglycans, Instructive Biomolecules That Regulate Cellular Activity and Synaptic Neuronal Control of Specific Tissue Functional Properties.International journal of molecular sciences · 2025Review
- Extracellular matrix: Dystroglycan interactions-Roles for the dystrophin-associated glycoprotein complex in skeletal tissue dynamics.International journal of experimental pathology · 2025Review
- Molecular insights into cell signaling pathways in kidney stone formation.Urolithiasis · 2025Review
- Live cell optical super-resolution microscopy of dystroglycan mutants as a model for dystroglycanopathies in multiple cell lines.Frontiers in molecular biosciences · 2025Article
- Extracellular matrix dysregulation in aging, calcification, and cancer diseases: insights into cellular senescence, inflammation, and novel therapeutic strategies.International journal of biological sciences · 2025Review
- Cell surface glycan engineering reveals that matriglycan alone can recapitulate dystroglycan binding and function.Nature communications · 2022Article
- Lassa virus glycoprotein complex review: insights into its unique fusion machinery.Bioscience reports · 2022Review
- The extracellular matrix protein Agrin is expressed by osteoblasts and contributes to their differentiation.Cell and tissue research · 2021Article
- Heparan sulfate proteoglycans serve as alternative receptors for low affinity LCMV variants.PLoS pathogens · 2021Article
- High degree of conservation of the enzymes synthesizing the laminin-binding glycoepitope of α-dystroglycan.Open biology · 2021Article
- The role of basement membranes in cardiac biology and disease.Bioscience reports · 2021Review
- Article
- Identification and Modeling of a GT-A Fold in the α-Dystroglycan Glycosylating Enzyme LARGE1.Journal of chemical information and modeling · 2020Article
- Congenital myasthenic syndrome-associated agrin variants affect clustering of acetylcholine receptors in a domain-specific manner.JCI insight · 2020Article
- An improved method for culturing myotubes on laminins for the robust clustering of postsynaptic machinery.Scientific reports · 2020Article
- Engineering Extracellular Matrix Proteins to Enhance Cardiac Regeneration After Myocardial Infarction.Frontiers in bioengineering and biotechnology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Dystroglycan (DG) is an adhesion complex that links the cytoskeleton to the surrounding extracellular matrix in skeletal muscle and a wide variety of other tissues. It is composed of a highly glycosylated extracellular α-DG associated noncovalently with a transmembrane β-DG whose cytodomain interacts with dystrophin and its isoforms. Alpha-dystroglycan (α-DG) binds tightly and in a calcium-dependent fashion to multiple extracellular proteins and proteoglycans, each of which harbors at least one, or, more frequently, tandem arrays of laminin-globular (LG) domains. Considerable biochemical and structural work has accumulated on the α-DG-binding LG domains, highlighting a significant heterogeneity in ligand-binding properties of domains from different proteins as well as between single and multiple LG domains within the same protein. Here we review biochemical, structural, and functional information on the LG domains reported to bind α-dystroglycan. In addition, we have incorporated bioinformatics and modeling to explore whether specific motifs responsible for α-dystroglycan recognition can be identified within isolated LG domains. In particular, we analyzed the LG domains of slits and agrin as well as those of paradigmatic α-DG non-binders such as laminin-α3. While some stretches of basic residues may be important, no universally conserved motifs could be identified. However, the data confirm that the coordinated calcium atom within the LG domain is needed to establish an interaction with the sugars of α-DG, although it appears that this alone is insufficient to mediate significant α-DG binding. We develop a scenario involving different binding modes of a single LG domain unit, or tandemly repeated units, with α-DG. A variability of binding modes might be important to generate a range of affinities to allow physiological regulation of this interaction, reflecting its crucial biological importance.
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