[SMC] Polymerizing laminins in development, health, and disease

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J Biol Chem. 2024 Jul;300(7):107429. doi: 10.1016/j.jbc.2024.107429. Epub 2024 Jun 1.

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.

PMID:38825010 | PMC:PMC11260871 | DOI:10.1016/j.jbc.2024.107429


Source: https://pubmed.ncbi.nlm.nih.gov/3882501 ... t9+e462414