- 著者
- Masako Koyama Yoshiyuki Matsuura
- 出版者
- The Biophysical Society of Japan
- 雑誌
- BIOPHYSICS (ISSN:13492942)
- 巻号頁・発行日
- vol.8, pp.145-150, 2012 (Released:2012-11-30)
- 参考文献数
- 24
- 被引用文献数
- 1 4
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.