Mutations of phosphorylation sites in lamin A that prevent nuclear lamina disassembly in mitosis

Cell. 1990 May 18;61(4):579-89. doi: 10.1016/0092-8674(90)90470-y.


The nuclear envelope is a dynamic structure that completely disassembles in response to MPF/cdc2 activity in mitosis. A key feature of this process is the hyperphosphorylation of the major structural proteins of the envelope, the nuclear lamins A, B, and C. Two highly conserved serine residues of the lamin protein (Ser-22 and Ser-392 of lamins A and C) are symmetrically positioned 5 amino acids from the ends of the large alpha-helical domain and are shown in the accompanying paper by Ward and Kirschner to be among four sites phosphorylated during nuclear envelope breakdown. Mutations in Ser-22 and Ser-392 that prevent phosphorylation at these sites block the disassembly of the nuclear lamina during mitosis. We propose a model for the regulation of lamin assembly in which phosphorylation just outside the ends of the alpha-helical domain controls the assembly dynamics of the lamin coiled-coil dimers.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cells, Cultured
  • Humans
  • Lamin Type A
  • Lamins
  • Macromolecular Substances
  • Mitosis / physiology*
  • Molecular Sequence Data
  • Mutation
  • Nuclear Envelope / metabolism*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Phenotype
  • Phosphorylation
  • Recombinant Proteins / metabolism
  • Structure-Activity Relationship
  • Transfection


  • Lamin Type A
  • Lamins
  • Macromolecular Substances
  • Nuclear Proteins
  • Recombinant Proteins