Nuclear assembly

Tracey Michele Gant, Katherine L. Wilson

Research output: Contribution to journalReview articlepeer-review

Abstract

We review old and new insights into the structure of the nuclear envelope and the components responsible for its dynamic reassembly during mitosis. New information is coming to light about several of the proteins that mediate nuclear reassembly. These proteins include the lamins and their emerging relationship with proteins such as otefin and the MAN antigens: peripheral proteins that might participate in lamina structure. There are four identified proteins localized to the inner nuclear membrane: the lamina- associated proteins LAP1 and LAP2, emerin, and the lamin B receptor (LBR). LBR can interact independently with lamin B and a chromodomain protein, Hp1, and appears to be a central player in targeting nuclear membranes to chromatin. Intermediates in the assembly of nuclear pore complexes (NPCs) can now be studied biochemically and visualized by high resolution scanning electron microscopy. We discuss the possibility that the filament-forming proteins Tpr/p270, NUMA, and perhaps actin may have roles in nuclear assembly.

Original languageEnglish (US)
Pages (from-to)669-695
Number of pages27
JournalAnnual Review of Cell and Developmental Biology
Volume13
DOIs
StatePublished - 1997

Keywords

  • Cell cycle
  • Emerin
  • LAP1
  • LAP2
  • LBR
  • Nuclear envelope
  • Nuclear lamina
  • Nuclear pore complexes
  • Nucleoskeleton

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology

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