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First published online October 30, 2006
doi: 10.1242/10.1242/jcs.03207
Research Article |
1 Cellular Dynamics Laboratory, Discovery Research Institute, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama, 351-0198 Japan
2 Department of Molecular Biology, BIKEN, Osaka University, Osaka, Japan
3 Laboratory for Neural Architecture, Brain Research Institute, RIKEN, Wako-shi, Japan
4 Department of Bioengineering, Graduate School of Engineering, Osaka City University, Osaka, Japan
* Authors for correspondence (e-mail: maeshima{at}riken.jp; nimamoto{at}riken.jp)
Accepted 9 August 2006
Nuclear pores are sophisticated gateways on the nuclear envelope that control macromolecular transport between the cytoplasm and nucleoplasm. So far the structural and functional aspects of nuclear pores have been extensively studied, but their distribution and density, which might reflect nuclear organization and function, remain unknown. Here, we report the cell-cycle-dependent dynamics of nuclear pores. Large distinct subdomains lacking nuclear pores are present on the nuclear surface of HeLaS3 cells in early cell-cycle stages. Such `pore-free islands' gradually become dispersed in G1-S phase. Surprisingly, the islands are enriched with inner nuclear membrane proteins lamin A/C and emerin, but exclude lamin B. Lamin-A/C-enriched pore-free islands were also observed in human normal diploid fibroblasts and several cell lines, showing the generality of this phenomenon. Knockdown and ectopic expression analyses demonstrated that lamin A/C, but not emerin, plays an essential structural and regulatory role in the nuclear pore distribution and the formation of pore-free islands. These data thus provide strong evidence that the dynamics of nuclear pores are regulated by the reorganization of inner nuclear structures.
Key words: Emerin, Cell cycle, Lamin A/C and lamin B, Nuclear pores, Nuclear structure
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