期刊
BIOCHEMICAL JOURNAL
卷 468, 期 -, 页码 353-362出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20150368
关键词
Importin; Karyopherin; nuclear import; nuclear localization signal (NLS); nuclear pore; nucleocytoplasmic transport
资金
- National Institutes of Health [R01-GM069909, U01 GM98256-01]
- Welch Foundation [I-1532]
- Cancer Prevention Research Institute of Texas (CPRIT) [RP150053]
- Leukemia and Lymphoma Society
- UT Southwestern Endowed Scholars Program
The Karyopherin-beta family of proteins mediates nuclear transport of macromolecules. Nuclear versus cytoplasmic localization of proteins is often suggested by the presence of NLSs (nuclear localization signals) or NESs (nuclear export signals). Import-Karyopherin-beta s or Importins bind to NLSs in their protein cargos to transport them through nuclear pore complexes into the nucleus. Until recently, only two classes of NLS had been biochemically and structurally characterized: the classical NLS, which is recognized by the Importin-alpha/beta heterodimer and the PY-NLS (proline-tyrosine NLS), which is recognized by Karyopherin-beta 2 or Transportin-1. Structures of two other Karyopherin-beta s, Kap121 and Transportin-SR2, in complex with their respective cargos were reported for the first time recently, revealing two new distinct classes of NLSs. The present paper briefly describes the classical NLS, reviews recent literature on the PY-NLS and provides in-depth reviews of the two newly discovered classes of NLSs that bind Kap121p and Transportin-SR respectively.
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