The Yeast Nuclear Pore Complex

By Michael P. Rout, J. Aitchison, Adisetyantari Suprapto, Kelly Hjertaas, Yingming Zhao, Brian T. Chait. Journal of Cell Biology, 2000

1,388 citations recorded by the source corpus.

An understanding of how the nuclear pore complex (NPC) mediates nucleocytoplasmic exchange requires a comprehensive inventory of the molecular components of the NPC and a knowledge of how each component contributes to the overall structure of this large molecular translocation machine. Therefore, we have taken a comprehensive approach to classify all components of the yeast NPC (nucleoporins). This involved identifying all the proteins present in a highly enriched NPC fraction, determining which of these proteins were nucleoporins, and localizing each nucleoporin within the NPC. Using these data, we present a map of the molecular architecture of the yeast NPC and provide evidence for a Brownian affinity gating mechanism for nucleocytoplasmic transport.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6615e191344bc14a39e3c74f688f27b804d4bdbe

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In Molecular Biology

1. J. Massagué
2. J. Seoane
3. Michael P. Rout
4. D. Wotton
5. I. Macara
6. D. Görlich
7. Katharina Ribbeck
8. B. Cravatt

Citations in the corpus

• Mechanisms of Receptor‐Mediated Nuclear Import and Nuclear Export (2005, background): “Proteomic characterization of the mammalian and yeast NPC has shown that it comprises approximately 30 proteins (53,54).”
• The biological impact of mass-spectrometry-based proteomics (2007, background): “In addition to the examples discussed in this section, other notable studies that have used mass-spectrometry-based proteomics to characterize protein complexes are described in refs”
• Proteomic analysis of the mammalian nuclear pore complex (2002, background): “A proteomic analysis revealed that the yeast NPC is composed of 29 nucleoporins (Rout et al., 2000).”
• The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion (2002, background): “The data argue against a key element of the Brownian af®nity gate model (Rout et al., 2000), in which Phe-rich repeats facilitate NPC passage only by feeding substrates into a rigid, narrow central channel.”
• The nuclear pore complex: bridging nuclear transport and gene regulation (2010, background): “FG Nups can be classified into two groups: symmetric, which are found on both sides of the NPC (for example NUP62 ), and asymmetric, which are found further from the central plane of the nuclear envelope and have a clear nuclear or cytoplasmic bias (for example NUP153”
• Smad transcription factors. (2005, background): “The intrinsic asymmetry of the nuclear pore complex, and the distribution of different nucleoporins along the span of the pore, are thought to allow proteins docking on one side of the pore to move unidirectionally to the other side and vice versa (Rout et al. 2000).”