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Updated: Aug 11, 2026
12:04
Examination of Mitotic and Meiotic Fission Yeast Nuclear Dynamics by Fluorescence Live-cell Microscopy
Published on: June 24, 2019
The yeast nuclear pore complex: composition, architecture, and transport mechanism
M P Rout1, J D Aitchison, A Suprapto
1The Rockefeller University, New York, NY 10021, USA. rout@rockvax.rockefeller.edu
The Journal of Cell Biology
|February 23, 2000
Summary
Researchers inventoried yeast nuclear pore complex (NPC) proteins to map its molecular architecture. This study reveals a Brownian affinity gating mechanism for nucleocytoplasmic transport.
Area of Science:
- Molecular Biology
- Cell Biology
- Biophysics
Background:
- The nuclear pore complex (NPC) regulates transport between the nucleus and cytoplasm.
- Understanding NPC function requires detailed knowledge of its molecular composition and architecture.
Purpose of the Study:
- To comprehensively classify all components of the yeast NPC (nucleoporins).
- To map the molecular architecture of the yeast NPC.
- To elucidate the mechanism of nucleocytoplasmic transport.
Main Methods:
- Proteomic analysis of highly enriched yeast NPC fractions.
- Identification and classification of nucleoporins.
- Localization of nucleoporins within the NPC structure.
Main Results:
- A comprehensive inventory of yeast nucleoporins was established.
- The molecular architecture of the yeast NPC was mapped.
- Evidence supporting a Brownian affinity gating mechanism for transport was provided.
Conclusions:
- The study provides a detailed molecular map of the yeast NPC.
- The findings offer insights into the mechanism of nucleocytoplasmic transport.
- The Brownian affinity gating model is proposed for NPC function.
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