Toward understanding the structure of the vertebrate nuclear pore complex

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: :

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

This article refers to:

10.4161/nucl.28739

Disclosure of Potential Conflicts of Interest

No potential conflict of interest was disclosed.

Acknowledgments

M.B. acknowledges funding by the European Research Council (309271-NPCAtlas).