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Yeast and vertebrate nuclear-pore complexes: evolutionary conserved, yet divergent macromolecular assemblies

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Summary

The nuclear-pore complex (NPC), which consists of ca. 50 proteins called nucleoporins, is a huge macromolecular structure that spans the nuclear envelope and is an obligatory passage for molecules in transit between the cytoplasm and the nucleus. In the last years, major progress has allowed the characterization of the so-called “soluble phase’ of nucleocytoplasmic transport, that involves transport substrates, import and export receptors of which some belong to the karyopherin-β family, and the small GTPase Ran and its modulators. In addition, the knowledge of the NPC architecture, the identification of its constituents, and the determination of the hierarchy of interactions within the pore should help to understand how nucleoporins are assembled, and how they give rise to a functional NPC through interactions with specific transport factors. In this review, we will focus on recent insights into the stationary phase of nucleocytoplasmic transport (i.e., the NPCs) that have been gained from exploiting the benefits of several organisms, such asXenopus laevis oocytes, mammalian cell lines, and the yeastSaccharomyces cerevisiae.

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Abbreviations

FXFG:

phenylalanine X phenylalanine glycine

GLFG:

glycine leucine phenylalanine glycine

NPC:

nuclear-pore complex

RLNE:

rat liver nuclear envelope

WGA:

wheat germ agglutinin

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  1. UMR 144 du CNRS, Institut Curie, 26 rue d'Ulm, F-75248, Paris Cedex 05, France

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Belgareh, N., Doye, V. Yeast and vertebrate nuclear-pore complexes: evolutionary conserved, yet divergent macromolecular assemblies. Protoplasma 209, 133–143 (1999). https://doi.org/10.1007/BF01453442

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