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-2521
Mol Cell 2005 Jan 07;171:83-92. doi: 10.1016/j.molcel.2004.12.010.
Show Gene links Show Anatomy links

The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation.

Antonin W , Franz C , Haselmann U , Antony C , Mattaj IW .


Abstract
The metazoan nuclear envelope (NE) breaks down and reforms at each mitosis. Nuclear pore complexes (NPCs), which allow nucleocytoplasmic transport during interphase, assemble into the reforming NE at the end of mitosis. Using in vitro NE assembly assays, we show that one of the two transmembrane nucleoporins, pom121, is essential for NE formation, whereas the second, gp210, is dispensable. Depletion of either pom121-containing membrane vesicles or the protein alone does not affect vesicle binding to chromatin but prevents their fusion to form a closed NE. When the Nup107-160 complex, which is essential for integration of NPCs into the NE, is also depleted, pom121 becomes dispensable for NE formation, suggesting a close functional link between NPC and NE formation and the existence of a checkpoint that monitors NPC assembly state.

PubMed ID: 15629719
Article link: Mol Cell


Species referenced: Xenopus laevis
Genes referenced: nup107 nup210 pom121 ranbp2
Antibodies: POM121 Ab1 Ranbp2 Ab1