Scaffold, mechanics and functions of nuclear lamins

Amnon Buxboim*, Rafael Kronenberg-Tenga, Sarka Salajkova, Nili Avidan, Hen Shahak, Alice Thurston, Ohad Medalia*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

4 Scopus citations

Abstract

Nuclear lamins are type-V intermediate filaments that are involved in many nuclear processes. In mammals, A- and B-type lamins assemble into separate physical meshwork underneath the inner nuclear membrane, the nuclear lamina, with some residual fraction localized within the nucleoplasm. Lamins are the major part of the nucleoskeleton, providing mechanical strength and flexibility to protect the genome and allow nuclear deformability, while also contributing to gene regulation via interactions with chromatin. While lamins are the evolutionary ancestors of all intermediate filament family proteins, their ultimate filamentous assembly is markedly different from their cytoplasmic counterparts. Interestingly, hundreds of genetic mutations in the lamina proteins have been causally linked with a broad range of human pathologies, termed laminopathies. These include muscular, neurological and metabolic disorders, as well as premature aging diseases. Recent technological advances have contributed to resolving the filamentous structure of lamins and the corresponding lamina organization. In this review, we revisit the multiscale lamin organization and discuss its implications on nuclear mechanics and chromatin organization within lamina-associated domains.

Original languageAmerican English
Pages (from-to)2791-2805
Number of pages15
JournalFEBS Letters
Volume597
Issue number22
DOIs
StatePublished - Nov 2023

Bibliographical note

Publisher Copyright:
© 2023 Federation of European Biochemical Societies.

Keywords

  • intermediate filaments
  • lamins
  • mechanobiology
  • nuclear lamina
  • progeria

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