Proteomic analysis of the mammalian nuclear pore complex

Janet M. Cronshaw, Andrew N. Krutchinsky, Wenzhu Zhang, Brian T. Chait, Michae L.J. Matunis

Research output: Contribution to journalArticlepeer-review

730 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)915-927
Number of pages13
JournalJournal of Cell Biology
Issue number5
StatePublished - Sep 2 2002


  • Nuclear pore complex
  • Nucleocytoplasmic transport
  • Nucleoporins
  • Proteomics
  • WD repeats

ASJC Scopus subject areas

  • Cell Biology


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