Phosphorylation of lamins determine their structural properties and signaling functions

Nucleus. 2015;6(3):166-71. doi: 10.1080/19491034.2015.1017167. Epub 2015 Mar 20.


Lamin A/C is part of the nuclear lamina, a meshwork of intermediate filaments underlying the inner nuclear membrane. The lamin network is anchoring a complex set of structural and linker proteins and is either directly or through partner proteins also associated or interacting with a number of signaling protein and transcription factors. During mitosis the nuclear lamina is dissociated by well established phosphorylation- dependent mechanisms. A-type lamins are, however, also phosphorylated during interphase. A recent study identified 20 interphase phosphorylation sites on lamin A/C and explored their functions related to lamin dynamics; movements, localization and solubility. Here we discuss these findings in the light of lamin functions in health and disease.

Keywords: EDMD, Emery-Dreifuss muscular dystrophy; GFP, green fluorescent protein; IFs, intermediate filaments; LAP2α, Lamina-associated polypeptide 2 isoform α; intermediate filaments; lamin A/C; laminopathy; lamins; phosphorylation; signaling.

MeSH terms

  • Animals
  • Caenorhabditis elegans / genetics
  • Caenorhabditis elegans / metabolism
  • Gene Expression Regulation
  • HeLa Cells
  • Humans
  • Intermediate Filaments / chemistry
  • Intermediate Filaments / metabolism
  • Interphase / genetics*
  • Lamin Type A / chemistry*
  • Lamin Type A / genetics
  • Lamin Type A / metabolism
  • Mitosis*
  • Muscular Dystrophy, Emery-Dreifuss / genetics*
  • Muscular Dystrophy, Emery-Dreifuss / metabolism
  • Muscular Dystrophy, Emery-Dreifuss / pathology
  • Mutation
  • Nuclear Lamina / chemistry
  • Nuclear Lamina / metabolism
  • Phosphorylation
  • Protein Transport
  • Signal Transduction*
  • Solubility


  • LMNA protein, human
  • Lamin Type A