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A more recent version of this article appeared on July 1, 2004
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Submitted on December 9, 2003
Revised on May 3, 2004
Accepted on May 4, 2004
, , 
, ||, , , *
UMR 144 CNRS-Institut Curie, Section Recherche, 26 Rue d'Ulm, 75248 Paris Cedex 05, France; Gene Expression and Cell Biology/Biophysics Programmes, EMBL, Meyerhofstrasse 1, 69117 Heidelberg, Germany
Monitoring Editor: Pamela Silver
In eukaryotes, bidirectional transport of macromolecules between the cytoplasm and the nucleus occurs through elaborate supramolecular structures embedded in the nuclear envelope, the nuclear pore complexes (NPCs). NPCs are composed of multiple copies of 
30 different proteins termed nucleoporins, of which several can be biochemically isolated as subcomplexes. One such building block of the NPC, termed the Nup107-160 complex in vertebrates, was so far demonstrated to be composed of six different nucleoporins. Here, we identify three WD (Trp-Asp)-repeat nucleoporins as new members of this complex, two of which, Nup37 and Nup43, are specific to higher eukaryotes. The third new member Seh1 is more loosely associated with the Nup107-160 complex biochemically, but its depletion by RNAi leads to phenotypes similar to knock down of other constituents of this complex. By combining GFP-tagged nucleoporins and specific antibodies, we show that all the constituents of this complex - including Nup37, Nup43, Seh1 and Sec13 - are targeted to kinetochores from prophase to anaphase of mitosis. Together, our results indicate that the entire Nup107-160 complex, that comprises nearly one third of the so-far identified nucleoporins, specifically localizes to kinetochores in mitosis.
present address: Department of Cell and Developmental Biology, University of Pennsylvania, Building BRB2/3, 421, Curie Boulevard, Philadelphia, PA, USA
||present address: The Laboratory for Cell Biology and Genetics, The Rockefeller University, 1230 York Ave, New York, USA
*Corresponding author. E-mail address: vdoye{at}curie.fr
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