2012年
Mechanistic insights from the recent structures of the CRM1 nuclear export complex and its disassembly intermediate
Biophysics (Japan)
- ,
- 巻
- 8
- 号
- 開始ページ
- 145
- 終了ページ
- 150
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.2142/biophysics.8.145
CRM1 (also known as exportin 1 or Xpo1) is the most versatile nuclear export receptor (exportin) that carries a broad range of proteins and ribonucleoproteins from the nucleus to the cytoplasm through the nuclear pore complex. The majority of the export substrates of CRM1 contain a short peptide sequence, so-called leucine-rich nuclear export signal (NES), which typically harbor four or five characteristically spaced hydrophobic residues. The transport directionality is determined by the small GTPase Ran and Ran-binding proteins that control the binding and dissociation of cargo. Here we review recent structural studies that advanced understanding of how NES is specifically recognized by CRM1 in the nucleus, and how NES is rapidly dissociated from CRM1 in the cytoplasm. © 2012 THE BIOPHYSICAL SOCIETY OF JAPAN.
- ID情報
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- DOI : 10.2142/biophysics.8.145
- ISSN : 1349-2942
- PubMed ID : 27493531
- SCOPUS ID : 84870729256