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Published online 26 August 2002. doi:10.1083/jcb.200206106
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© The Rockefeller University Press, 0021-9525/2002/9/915 $5.00
The Journal of Cell Biology, Volume 158, Number 5, September 2, 2002 915-927

Article

Proteomic analysis of the mammalian nuclear pore complex



Janet M. Cronshaw1, Andrew N. Krutchinsky2, Wenzhu Zhang2, Brian T. Chait2 and Michael J. Matunis1

1 Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205
2 Laboratory of Mass Spectrometry and Gaseous Ion Chemistry, Rockefeller University, New York, NY 10021

Address correspondence to Michael Matunis, Dept. of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, 615 N. Wolfe St., Baltimore, MD 21205. Tel.: (410) 614-6878. Fax: (410) 955-2926. E-mail: mmatunis{at}jhsph.edu

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.

Key Words: nuclear pore complex; nucleoporins; nucleocytoplasmic transport; proteomics; WD repeats


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