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Related Experiment Video

Updated: Jun 20, 2026

Single-Molecule Imaging of Nuclear Transport

Single-Molecule Imaging of Nuclear Transport

Published on: June 9, 2010

Diffusion of large molecules into assembling nuclei revealed using an optical highlighting technique.

Satoshi Shimozono¹, Hidekazu Tsutsui, Atsushi Miyawaki

¹Laboratory for Cell Function Dynamics, Advanced Technology Development Group, Brain Science Institute, Institute of Physical and Chemical Research, Saitama, Japan.

Biophysical Journal

|September 2, 2009

Summary

Newly formed nuclei allow large proteins to enter during reassembly after mitosis. This challenges the established understanding of nuclear pore complex diffusion barriers.

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Single-Molecule Imaging of Nuclear Transport

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Published on: June 9, 2010

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Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization

Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization

Published on: February 3, 2013

Area of Science:

Cell Biology
Molecular Biology
Biophysics

Background:

The nuclear envelope (NE) separates the nucleus from the cytoplasm, with nuclear pore complexes (NPCs) regulating molecular transport.
NPCs typically allow passive diffusion of proteins <50 kDa, while excluding larger proteins (>60 kDa).
The dynamics of this size exclusion during NE reassembly post-mitosis remain poorly understood.

Purpose of the Study:

To investigate the permeability of the reassembling nuclear envelope to large proteins.
To determine if the established NPC size cutoff applies during the immediate post-mitotic period.

Main Methods:

Utilized the tetrameric photoconvertible fluorescent protein KikGR (103 kDa) as a model large protein.
Optically highlighted KikGR in the cytoplasm and tracked its diffusion into newly forming nuclei post-cytokinesis.

Main Results:

Remarkably, the 103 kDa KikGR complex efficiently entered newly assembled nuclei within 20 minutes after cytokinesis.
KikGR lacks known nuclear localization signals or chromosome-binding domains, suggesting entry is not due to specific targeting.
This efficient entry indicates a less restrictive diffusion barrier during the nuclear envelope reassembly phase.

Conclusions:

The nuclear envelope's diffusion barrier is significantly more permeable to large proteins during the immediate post-mitotic reassembly phase than previously assumed.
Established models of NPC-mediated size exclusion may not fully apply during this transient nuclear assembly period.
Further research is needed to elucidate the mechanisms governing this transient permeability and its biological implications.