MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly

EMBO Rep. 2007 Feb;8(2):165-72. doi: 10.1038/sj.embor.7400889. Epub 2007 Jan 19.


The metazoan nuclear envelope (NE) breaks down and re-forms during each cell cycle. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport during interphase, assemble into the re-forming NE at the end of mitosis. Using in vitro NE assembly, we show that the vertebrate homologue of MEL-28 (maternal effect lethal), a recently discovered NE component in Caenorhabditis elegans, functions in postmitotic NPC assembly. MEL-28 interacts with the Nup107-160 complex (Nup for nucleoporin), an important building block of the NPC, and is essential for the recruitment of the Nup107-160 complex to chromatin. We suggest that MEL-28 acts as a seeding point for NPC assembly.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins / metabolism*
  • Cell Cycle / physiology*
  • Chromatin / metabolism*
  • DNA-Binding Proteins
  • Escherichia coli
  • Fluorescent Antibody Technique
  • Humans
  • Nuclear Pore / metabolism*
  • Nuclear Pore Complex Proteins / metabolism*
  • Nuclear Proteins / metabolism*
  • RNA Interference
  • RNA, Small Interfering / genetics
  • Xenopus


  • Caenorhabditis elegans Proteins
  • Chromatin
  • DNA-Binding Proteins
  • Nuclear Pore Complex Proteins
  • Nuclear Proteins
  • RNA, Small Interfering
  • mel-28 protein, C elegans