Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex

@article{Berke2004StructuralAF,
  title={Structural and functional analysis of Nup133 domains reveals modular building blocks of the nuclear pore complex},
  author={Ian C. Berke and Thomas Boehmer and G{\"u}nter Blobel and Thomas U Schwartz},
  journal={The Journal of Cell Biology},
  year={2004},
  volume={167},
  pages={591 - 597}
}
Nucleocytoplasmic transport occurs through nuclear pore complexes (NPCs) whose complex architecture is generated from a set of only approximately 30 proteins, termed nucleoporins. Here, we explore the domain structure of Nup133, a nucleoporin in a conserved NPC subcomplex that is crucial for NPC biogenesis and is believed to form part of the NPC scaffold. We show that human Nup133 contains two domains: a COOH-terminal domain responsible for its interaction with its subcomplex through Nup107… CONTINUE READING

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Components of coated vesicles and nuclear pore complexes share a common molecular architecture

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  • PLoS Biol. doi: 10.1371/ journal.pbio.0020380
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