Proteomic analysis of the mammalian nuclear pore complex

doi:10.1083/jcb.200206106

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 nuclearpore complex (NPC) has a vital cellular role. Nonetheless, muchremains to be learned about many fundamental aspects of NPCfunction. To further understand the structure and function ofthe mammalian NPC, we have completed a proteomic analysis toidentify and classify all of its protein components. We usedmass spectrometry to identify all proteins present in a biochemicallypurified NPC fraction. Based on previous characterization, sequencehomology, and subcellular localization, 29 of these proteinswere classified as nucleoporins, and a further 18 were classifiedas NPC-associated proteins. Among the 29 nucleoporins were sixpreviously undiscovered nucleoporins and a novel family of WDrepeat nucleoporins. One of these WD repeat nucleoporins isALADIN, the gene mutated in triple-A (or Allgrove) syndrome.Our analysis defines the proteome of the mammalian NPC for thefirst time and paves the way for a more detailed characterizationof NPC structure and function.

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

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