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Nuclear pore complex proteins

R Bastos1, N Panté, B Burke

  • 1Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.

International Review of Cytology
|January 1, 1995
PubMed
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The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm. This review summarizes known NPC proteins and their functions in nucleocytoplasmic transport.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The nuclear envelope separates the nucleus and cytoplasm, controlling macromolecule exchange.
  • Nuclear pore complexes (NPCs) are intricate channels mediating this nucleocytoplasmic transport.
  • Vertebrate NPCs are massive structures (~120 MDa) composed of numerous polypeptide subunits.

Purpose of the Study:

  • To identify NPC subunits and elucidate their functions and interactions.
  • To understand the three-dimensional structure of the NPC.
  • To review current knowledge of approximately 20 described NPC proteins from vertebrate and yeast cells.

Main Methods:

  • Literature review of published studies on nuclear pore complex proteins.
  • Analysis of protein identification and functional characterization data.

Related Experiment Videos

  • Compilation of structural information regarding NPC assembly.

    • Main Results:

    • Approximately 20 distinct nuclear pore complex proteins have been identified in vertebrate and yeast cells.
    • These proteins play crucial roles in regulating nucleocytoplasmic transport.
    • Emerging data suggests complex interactions and a defined 3D organization of NPC components.

    Conclusions:

    • Understanding NPC protein composition and function is key to deciphering nucleocytoplasmic transport.
    • Further research is needed to fully characterize all NPC subunits and their roles.
    • This review provides a foundational summary of the current state of knowledge in the field.