The nuclear lamina comes of age

Nat Rev Mol Cell Biol. 2005 Jan;6(1):21-31. doi: 10.1038/nrm1550.


Many nuclear proteins form lamin-dependent complexes, including LEM-domain proteins, nesprins and SUN-domain proteins. These complexes have roles in chromatin organization, gene regulation and signal transduction. Some link the nucleoskeleton to cytoskeletal structures, ensuring that the nucleus and centrosome assume appropriate intracellular positions. These complexes provide new insights into cell architecture, as well as a foundation for the understanding of the molecular mechanisms that underlie the human laminopathies - clinical disorders that range from Emery-Dreifuss muscular dystrophy to the accelerated ageing seen in Hutchinson-Gilford progeria syndrome.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Actins / physiology
  • Aging / metabolism
  • Animals
  • Centrosome / physiology
  • Cytoskeleton / physiology
  • DNA-Binding Proteins
  • Humans
  • Lamins / physiology*
  • Membrane Proteins / physiology
  • Muscular Dystrophies / etiology
  • Muscular Dystrophies / metabolism
  • Nuclear Lamina / physiology*
  • Nuclear Proteins / physiology
  • Signal Transduction / physiology
  • Thymopoietins / physiology


  • Actins
  • DNA-Binding Proteins
  • LEMD3 protein, human
  • Lamins
  • Membrane Proteins
  • Nuclear Proteins
  • Thymopoietins
  • emerin