Karyopherins are a group of proteins involved in transporting molecules between the cytoplasm and the nucleus of a eukaryotic cell. The inside of the nucleus is called the karyoplasm (or nucleoplasm). Generally, karyopherin-mediated transport occurs through the nuclear pore, which acts as a gateway into and out of the nucleus. Most proteins require karyopherins to traverse the nuclear pore.
Karyopherins can act as importins (i.e. helping proteins get into the nucleus) or exportins (i.e. helping proteins get out of the nucleus). They belong to The Nuclear Pore Complex Family in the transporter classification database (TCDB).
Energy for transport is derived from the Ran gradient. See Ran for further details.
Importin beta is a specific type of karyopherin that facilitates the transport of cargo proteins into the nucleus. First, it is binding importin alpha - another type of karyopherin that binds the cargo protein in the cytoplasm - before the cargo protein is imported into the nucleus through the nuclear pore using energy derived from the Ran gradient. Once inside the nucleus, the cargo dissociates from the karyopherins.
Human genes in the karyopherin family
- Mahboubi, Hicham; Seganathy, Evangeline; Kong, Dekun; Stochaj, Ursula (2013-06-27). "Identification of Novel Stress Granule Components That Are Involved in Nuclear Transport". PLoS ONE. 8 (6): e68356. doi:10.1371/journal.pone.0068356. PMC . PMID 23826389.
- Fujimura, Ken; Suzuki, Tomonori; Yasuda, Yoshinari; Murata, Masayuki; Katahira, Jun; Yoneda, Yoshihiro (2010-07-01). "Identification of importin α1 as a novel constituent of RNA stress granules". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1803 (7): 865–871. doi:10.1016/j.bbamcr.2010.03.020.
- Poon, I. K. H. and D. A. Jans (2005). "Regulation of nuclear transport: Central role in development and transformation?" Traffic 6(3): 173-186.
- Karyopherins at the US National Library of Medicine Medical Subject Headings (MeSH)
- Illustrations at berkeley.edu
- Karyopherin animations
- Karyopherin illustrations
- 3D electron microscopy structures of exportin from the EM Data Bank(EMDB)
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