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Updated: Jun 24, 2025

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
Published on: September 28, 2020
Polymerizing laminins in development, health, and disease
Peter D Yurchenco1, Arkadiusz W Kulczyk2
1Department of Pathology & Laboratory Medicine, Robert Wood Johnson Medical School, Rutgers University, Piscataway, New Jersey, USA.
Abstract:
Polymerizing laminins are multi-domain basement membrane (BM) glycoproteins that self-assemble into cell-anchored planar lattices to establish the initial BM scaffold. Nidogens, collagen-IV and proteoglycans then bind to the scaffold at different domain loci to create a mature BM. The LN domains of adjacent laminins bind to each other to form a polymer node, while the LG domains attach to cytoskeletal-anchoring integrins and dystroglycan, as well as to sulfatides and heparan sulfates. The polymer node, the repeating unit of the polymer scaffold, is organized into a near-symmetrical triskelion. The structure, recently solved by cryo-electron microscopy in combination with AlphaFold2 modeling and biochemical studies, reveals how the LN surface residues interact with each other and how mutations cause failures of self-assembly in an emerging group of diseases, the LN-lamininopathies, that include LAMA2-related dystrophy and Pierson syndrome.
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