Proteomic analysis of the mammalian nuclear pore complex

J Cell Biol. 2002 Sep 2;158(5):915-27. doi: 10.1083/jcb.200206106. Epub 2002 Aug 26.


As the sole site of nucleocytoplasmic transport, the nuclear pore complex (NPC) has a vital cellular role. Nonetheless, much remains to be learned about many fundamental aspects of NPC function. To further understand the structure and function of the mammalian NPC, we have completed a proteomic analysis to identify and classify all of its protein components. We used mass spectrometry to identify all proteins present in a biochemically purified NPC fraction. Based on previous characterization, sequence homology, and subcellular localization, 29 of these proteins were classified as nucleoporins, and a further 18 were classified as NPC-associated proteins. Among the 29 nucleoporins were six previously undiscovered nucleoporins and a novel family of WD repeat nucleoporins. One of these WD repeat nucleoporins is ALADIN, the gene mutated in triple-A (or Allgrove) syndrome. Our analysis defines the proteome of the mammalian NPC for the first time and paves the way for a more detailed characterization of NPC structure and function.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Evolution, Molecular
  • HeLa Cells
  • Humans
  • Liver / cytology
  • Mass Spectrometry
  • Microscopy, Electron
  • Molecular Weight
  • Nuclear Pore / chemistry*
  • Nuclear Pore / metabolism*
  • Nuclear Pore / ultrastructure
  • Nuclear Pore Complex Proteins / analysis
  • Nuclear Pore Complex Proteins / chemistry*
  • Nuclear Pore Complex Proteins / classification
  • Nuclear Pore Complex Proteins / isolation & purification*
  • Proteomics*
  • Rats
  • Transfection


  • Nuclear Pore Complex Proteins