Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Journal Article

Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin.


Görlich,  D.
Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society;

External Resource
Fulltext (public)

(Publisher version), 464KB

Supplementary Material (public)

(Supplementary material), 186KB

(Supplementary material), 167KB

(Supplementary material), 168KB


Dean, K. A., von Ahsen, O., Görlich, D., & Fried, H. M. (2001). Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin. Journal of Cell Science, 114(19), 3479-3485.

Cite as: http://hdl.handle.net/11858/00-001M-0000-0015-3D81-6
The signal recognition particle (SRP) is a cytoplasmic RNA-protein complex that targets proteins to the rough endoplasmic reticulum. Although SRP functions in the cytoplasm, RNA microinjection and cDNA transfection experiments in animal cells, as well as genetic analyses in yeast, have indicated that SRP assembles in the nucleus. Nonetheless, the mechanisms responsible for nuclear-cytoplasmic transport of SRP RNA and SRP proteins are largely unknown. Here we show that the 19 kDa protein subunit of mammalian SRP, SRP19, was efficiently imported into the nucleus in vitro by two members of the importin β superfamily of transport receptors, importin 8 and transportin; SRP19 was also imported less efficiently by several other members of the importin β family. Although transportin is known to import a variety of proteins, SRP19 import is the first function assigned to importin 8. Furthermore, we show that a significant pool of endogenous SRP19 is located in the nucleus, as well as the nucleolus. Our results show that at least one mammalian SRP protein is specifically imported into the nucleus, by members of the importin β family of transport receptors, and the findings add additional evidence for nuclear assembly of SRP.