ArticleCommunications biology2022
Crystal structure of progeria mutant S143F lamin A/C reveals increased hydrophobicity driving nuclear deformation.
Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 8 citations in OpenAlex.
- Inflammation and Fibrosis in Progeria: Organ-Specific Responses in an HGPS Mouse Model.International journal of molecular sciences · 2024Article
- Lamin Filament Assembly Derived from the Atomic Structure of the Antiparallel Four-Helix Bundle.Molecules and cells · 2023Article
- Spf1 and Ste24: quality controllers of transmembrane protein topology in the eukaryotic cell.Frontiers in cell and developmental biology · 2023Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Lamins are intermediate filaments that form a 3-D meshwork in the periphery of the nuclear envelope. The recent crystal structure of a long fragment of human lamin A/C visualized the tetrameric assembly unit of the central rod domain as a polymerization intermediate. A genetic mutation of S143F caused a phenotype characterized by both progeria and muscular dystrophy. In this study, we determined the crystal structure of the lamin A/C fragment harboring the S143F mutation. The obtained structure revealed the X-shaped interaction between the tetrameric units in the crystals, potentiated by the hydrophobic interactions of the mutated Phe143 residues. Subsequent studies indicated that the X-shaped interaction between the filaments plays a crucial role in disrupting the normal lamin meshwork. Our findings suggest the assembly mechanism of the 3-D meshwork and further provide a molecular framework for understanding the aging process by nuclear deformation.
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