2012年11月
Karyopherin-independent spontaneous transport of amphiphilic proteins through the nuclear pore
JOURNAL OF CELL SCIENCE
- ,
- ,
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- 巻
- 125
- 号
- 21
- 開始ページ
- 4979
- 終了ページ
- 4984
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1242/jcs.109520
- 出版者・発行元
- COMPANY OF BIOLOGISTS LTD
Highly selective nucleocytoplasmic molecular transport is critical to eukaryotic cells, which is illustrated by size-filtering diffusion and karyopherin-mediated passage mechanisms. However, a considerable number of large proteins without nuclear localization signals are localized to the nucleus. In this paper, we provide evidence for the spontaneous migration of large proteins in a karyopherin-independent manner. Time-lapse observation of a nuclear transport assay revealed that several large molecules spontaneously and independently pass through the nuclear pore complex (NPC). The amphiphilic motifs were sufficient to overcome the selectivity barrier of the NPC. Furthermore, the amphiphilic property of these proteins enables altered local conformation in hydrophobic solutions so that elevated surface hydrophobicity facilitates passage through the nuclear pore. The molecular dynamics simulation revealed the conformational change of the amphiphilic structure that exposes the hydrophobic amino acid residues to the outer surface in a hydrophobic solution. These results contribute to the understanding of nucleocytoplasmic molecular sorting and the nature of the permeability barrier.
- リンク情報
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- DOI
- https://doi.org/10.1242/jcs.109520
- J-GLOBAL
- https://jglobal.jst.go.jp/detail?JGLOBAL_ID=201302215777270355
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/22946045
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000312984300005&DestApp=WOS_CPL
- ID情報
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- DOI : 10.1242/jcs.109520
- ISSN : 0021-9533
- J-Global ID : 201302215777270355
- PubMed ID : 22946045
- Web of Science ID : WOS:000312984300005