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Nucleus. 2014 Mar-Apr;5(2):119-23. doi: 10.4161/nucl.28739. Epub 2014 Apr 3.

Toward understanding the structure of the vertebrate nuclear pore complex.

Author information

1
European Molecular Biology Laboratory; Structural and Computational Biology Unit; Heidelberg, Germany; Stevens Institute of Technology; Department of Chemistry, Chemical Biology, and Biomedical Engineering; Hoboken, NJ USA.

Abstract

Nuclear pore complexes are large macromolecular assemblies that facilitate the nucleocytoplasmic exchange of macromolecules. Because of their intricate composition, membrane association, and sheer size, the integration of various, complementary structure determination approaches is a prerequisite for elucidating their structure. We have recently employed such an integrated strategy to analyze the scaffold structure of the cytoplasmic and nuclear rings of the human nuclear pore complex. In this extra view, we highlight two specific aspects of this work: the power of electron microscopy for bridging different resolution regimes and the importance of post-translational modifications for regulating nucleoporin interactions. We review recent technological developments and give a perspective toward future structure determination approaches.

KEYWORDS:

Cryo electron tomography; Nup107 subcomplex; nuclear pore complex; nucleoporins; phosphorylation

PMID:
24699243
PMCID:
PMC4049917
DOI:
10.4161/nucl.28739
[Indexed for MEDLINE]
Free PMC Article

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