The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis
Mol Biol Cell.. 2004-07-15; 15(7): 3333-44
DOI: 10.1091/mbc.E03-12-0878E03-12-0878 [pii]
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1. Mol Biol Cell. 2004 Jul;15(7):3333-44. Epub 2004 May 14.
The entire Nup107-160 complex, including three new members, is targeted as one
entity to kinetochores in mitosis.
Loïodice I(1), Alves A, Rabut G, Van Overbeek M, Ellenberg J, Sibarita JB, Doye V.
(1)Unité Mixte de Recherche 144 Centre National de la Recherche
Scientifique-Institut Curie, Section Recherche, 75248 Paris Cedex 05, France.
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 approximately 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 RNA interference leads to phenotypes similar to knock down of
other constituents of this complex. By combining green fluorescent protein-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, which comprises nearly one-third of the so-far
identified nucleoporins, specifically localizes to kinetochores in mitosis.