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Related Experiment Videos

Nuclear assembly

T M Gant1, K L Wilson

  • 1Department of Cell Biology and Anatomy, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Annual Review of Cell and Developmental Biology
|January 1, 1997
PubMed
Summary
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This review explores nuclear envelope structure and the proteins driving its reassembly during cell division. Key proteins like lamins, LAP1, LAP2, emerin, and LBR are crucial for nuclear membrane targeting and lamina structure.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The nuclear envelope disassembles during mitosis and reassembles around chromosomes.
  • Understanding the proteins involved in nuclear envelope reassembly is critical for cell division.
  • Previous knowledge on nuclear envelope structure and dynamics was limited.

Purpose of the Study:

  • To review current understanding of nuclear envelope structure.
  • To highlight proteins involved in nuclear envelope reassembly during mitosis.
  • To discuss emerging insights into lamina structure and nuclear membrane targeting.

Main Methods:

  • Literature review of existing and new research.
  • Biochemical studies of nuclear pore complex assembly intermediates.

Related Experiment Videos

  • High-resolution scanning electron microscopy visualization.

    • Main Results:

    • Identified key proteins in nuclear envelope reassembly: lamins, otefin, MAN antigens, LAP1, LAP2, emerin, and lamin B receptor (LBR).
    • LBR is a central protein targeting nuclear membranes to chromatin via interactions with lamin B and Hp1.
    • Filament-forming proteins like Tpr/p270, NuMA, and actin may play roles in nuclear assembly.

    Conclusions:

    • Proteins like otefin and MAN antigens are emerging as important for lamina structure.
    • LBR plays a pivotal role in connecting nuclear membranes to chromatin.
    • Further research is needed to elucidate the roles of Tpr/p270, NuMA, and actin in nuclear assembly.