Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-5377
Mol Cell. April 1, 2003; 11 (4): 853-64.

Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores.

Harel A , Orjalo AV , Vincent T , Lachish-Zalait A , Vasu S , Shah S , Zimmerman E , Elbaum M , Forbes DJ .


Abstract
The vertebrate nuclear pore complex, 30 times the size of a ribosome, assembles from a library of soluble subunits and two membrane proteins. Using immunodepletion of Xenopus nuclear reconstitution extracts, it has previously been possible to assemble nuclei lacking pore subunits tied to protein import, export, or mRNA export. However, these altered pores all still possessed the bulk of pore structure. Here, we immunodeplete a single subunit, the Nup107-160 complex, using antibodies to Nup85 and Nup133, two of its components. The resulting reconstituted nuclei are severely defective for NLS import and DNA replication. Strikingly, they show a profound defect for every tested nucleoporin. Even the integral membrane proteins POM121 and gp210 are absent or unorganized. Scanning electron microscopy reveals pore-free nuclei, while addback of the Nup107-160 complex restores functional pores. We conclude that the Nup107-160 complex is a pivotal determinant for vertebrate nuclear pore complex assembly.

PubMed ID: 12718872
Article link: Mol Cell.
Grant support: R01 GM33279 NIGMS NIH HHS

Genes referenced: nup107 nup133 nup210 nup85
Antibodies referenced:
Morpholinos referenced:

My Xenbase: [ Log-in / Register ]
version: [3.2.3]


Major funding for Xenbase is provided by the National Institute of Child Health and Human Development, grant P41 HD064556