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Abstract

Over the past two years, it has become evident that there is an unexpected link between nuclear pore complex structure and dynamics, nucleocytoplasmic transport and chromosome segregation. In addition, a tomographic three-dimensional reconstruction of native nuclear pore complexes preserved in thick amorphous ice has unveiled a number of new structural features of this supramolecular machine. These data, together with some of the elementary physical principles that underlie nucleocytoplasmic transport, will be discussed in this review.

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The way things move: looking under the hood of molecular motor proteins.

R D Vale, R Milligan (2000)

The microtubule-based kinesin motors and actin-based myosin motors generate motions associated with intracellular trafficking, cell division, and muscle contraction. Early studies suggested that these molecular motors work by very different mechanisms. Recently, however, it has become clear that kinesin and myosin share a common core structure and convert energy from adenosine triphosphate into protein motion using a similar conformational change strategy. Many different types of mechanical amplifiers have evolved that operate in conjunction with the conserved core. This modular design has given rise to a remarkable diversity of kinesin and myosin motors whose motile properties are optimized for performing distinct biological functions.

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The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion.

Katharina Ribbeck, Dirk Görlich (2002)

Nuclear pore complexes (NPCs) restrict the nucleocytoplasmic flux of most macromolecules, but permit facilitated passage of nuclear transport receptors and their cargo complexes. We found that a simple hydrophobic interaction column can mimic the selectivity of NPCs surprisingly well and that nuclear transport receptors appear to be the most hydrophobic soluble proteins. This suggests that surface hydrophobicity represents a major sorting criterion of NPCs. The rate of NPC passage of cargo-receptor complexes is, however, not dominated just by properties of the receptors. We found that large cargo domains drastically hinder NPC passage and require more than one receptor molecule for rapid translocation. This argues against a rigid translocation channel and instead suggests that NPC passage involves a partitioning of the entire translocating species into a hydrophobic phase, whereby the receptor:cargo ratio determines the solubility in that permeability barrier. Finally, we show that interfering with hydrophobic interactions causes a reversible collapse of the permeability barrier of NPCs, which is consistent with the assumption that the barrier is formed by phenylalanine-rich nucleoporin repeats that attract each other through hydrophobic interactions.

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Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm.

Nelly Panté, Michael Kann (2002)

Bidirectional transport of macromolecules between the nucleus and the cytoplasm occurs through the nuclear pore complexes (NPCs) by a signal-mediated mechanism that is directed by targeting signals (NLSs) residing on the transported molecules or "cargoes." Nuclear transport starts after interaction of the targeting signal with soluble cellular receptors. After the formation of the cargo-receptor complex in the cytosol, this complex crosses the NPC. Herein, we use gold particles of various sizes coated with cargo-receptor complexes to determine precisely how large macromolecules crossing the NPC by the signal-mediated transport mechanism could be. We found that cargo-receptor-gold complexes with diameter close to 39 nm could be translocated by the NPC. This implies that macromolecules much larger than the assumed functional NPC diameter of 26 nm can be transported into the karyoplasm. The physiological relevance of this finding was supported by the observation that intact nucleocapsids of human hepatitis B virus with diameters of 32 and 36 nm are able to cross the nuclear pore without disassembly.

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DOI:: 10.1038/nrm1230

PubMed ID:: 14570049

ScienceOpen disciplines: Chemistry

Keywords: Animals,ultrastructure,Nuclear Pore Complex Proteins,ran GTP-Binding Protein,Active Transport, Cell Nucleus,Models, Molecular,metabolism,physiology,Models, Biological,Nuclear Pore

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ScienceOpen disciplines: Chemistry

Keywords: Animals, ultrastructure, Nuclear Pore Complex Proteins, ran GTP-Binding Protein, Active Transport, Cell Nucleus, Models, Molecular, metabolism, physiology, Models, Biological, Nuclear Pore

The nuclear pore complex: nucleocytoplasmic transport and beyond.

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Abstract

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Most cited references 78

The way things move: looking under the hood of molecular motor proteins.

The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion.

Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm.

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