Fibrillin microfibril structure identifies long-range effects of inherited pathogenic mutations affecting a key regulatory latent TGFβ-binding site

Nat Struct Mol Biol. 2023 May;30(5):608-618. doi: 10.1038/s41594-023-00950-8. Epub 2023 Apr 20.

Abstract

Genetic mutations in fibrillin microfibrils cause serious inherited diseases, such as Marfan syndrome and Weill-Marchesani syndrome (WMS). These diseases typically show major dysregulation of tissue development and growth, particularly in skeletal long bones, but links between the mutations and the diseases are unknown. Here we describe a detailed structural analysis of native fibrillin microfibrils from mammalian tissue by cryogenic electron microscopy. The major bead region showed pseudo eightfold symmetry where the amino and carboxy termini reside. On the basis of this structure, we show that a WMS deletion mutation leads to the induction of a structural rearrangement that blocks interaction with latent TGFβ-binding protein-1 at a remote site. Separate deletion of this binding site resulted in the assembly of shorter fibrillin microfibrils with structural alterations. The integrin αvβ3-binding site was also mapped onto the microfibril structure. These results establish that in complex extracellular assemblies, such as fibrillin microfibrils, mutations may have long-range structural consequences leading to the disruption of growth factor signaling and the development of disease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Extracellular Matrix* / genetics
  • Extracellular Matrix* / metabolism
  • Fibrillin-1 / genetics
  • Fibrillin-1 / metabolism
  • Fibrillins / genetics
  • Fibrillins / metabolism
  • Mammals / metabolism
  • Microfibrils* / metabolism
  • Microfibrils* / pathology
  • Mutation
  • Transforming Growth Factor beta / genetics
  • Transforming Growth Factor beta / metabolism

Substances

  • Fibrillins
  • Transforming Growth Factor beta
  • Fibrillin-1