Protein-protein interactions between human nuclear lamins expressed in yeast

Exp Cell Res. 1995 Jul;219(1):292-8. doi: 10.1006/excr.1995.1230.


Protein-protein interactions between the nuclear lamins are responsible for the assembly of the nuclear lamina, a meshwork of intermediate filaments associated with the nuclear envelope inner membrane. We have used the yeast two-hybrid system to examine the interactions between the predominant human nuclear lamins expressed as GAL4 fusion proteins in Saccharomyces cerevisiae. Lamin A, prelamin A, lamin B1, and lamin C were able to form homodimers as well as heterodimers. Analysis of the different structural domains of lamin B1 demonstrated that the second half of coil 2 of the rod domain was necessary for the formation of the most stable homodimers. The results show that the yeast two-hybrid system can be used to study the interactions between structural proteins and their domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • DNA-Binding Proteins
  • Fungal Proteins / metabolism
  • Humans
  • Lamin Type A
  • Lamin Type B*
  • Lamins
  • Macromolecular Substances
  • Nuclear Envelope / metabolism
  • Nuclear Proteins / biosynthesis
  • Nuclear Proteins / metabolism*
  • Plasmids
  • Polymerase Chain Reaction
  • Recombinant Fusion Proteins / biosynthesis
  • Recombinant Fusion Proteins / metabolism*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Transcription Factors*
  • beta-Galactosidase / biosynthesis
  • beta-Galactosidase / metabolism*


  • DNA-Binding Proteins
  • Fungal Proteins
  • GAL4 protein, S cerevisiae
  • Lamin Type A
  • Lamin Type B
  • Lamins
  • Macromolecular Substances
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • lamin B1
  • lamin C
  • beta-Galactosidase