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XB-ART-39331
J Cell Biol 2009 Mar 09;1845:659-75. doi: 10.1083/jcb.200806174.
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ER membrane-bending proteins are necessary for de novo nuclear pore formation.

Dawson TR , Lazarus MD , Hetzer MW , Wente SR .


Abstract
Nucleocytoplasmic transport occurs exclusively through nuclear pore complexes (NPCs) embedded in pores formed by inner and outer nuclear membrane fusion. The mechanism for de novo pore and NPC biogenesis remains unclear. Reticulons (RTNs) and Yop1/DP1 are conserved membrane protein families required to form and maintain the tubular endoplasmic reticulum (ER) and the postmitotic nuclear envelope. In this study, we report that members of the RTN and Yop1/DP1 families are required for nuclear pore formation. Analysis of Saccharomyces cerevisiae prp20-G282S and nup133 Delta NPC assembly mutants revealed perturbations in Rtn1-green fluorescent protein (GFP) and Yop1-GFP ER distribution and colocalization to NPC clusters. Combined deletion of RTN1 and YOP1 resulted in NPC clustering, nuclear import defects, and synthetic lethality with the additional absence of Pom34, Pom152, and Nup84 subcomplex members. We tested for a direct role in NPC biogenesis using Xenopus laevis in vitro assays and found that anti-Rtn4a antibodies specifically inhibited de novo nuclear pore formation. We hypothesize that these ER membrane-bending proteins mediate early NPC assembly steps.

PubMed ID: 19273614
PMC ID: PMC2686408
Article link: J Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: dnai1 kdelr1 ndc1 nfyc nop2 nup133 nup153 nup214 nup62 pgk1 ranbp2 rtn1 rtn2 rtn4 tbx2 tfdp1
Antibodies: Ranbp2 Ab1


Article Images: [+] show captions
References [+] :
Aitchison, Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. 1995, Pubmed