DOI: 10.1242/jcs.114.19.3479. Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin

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

10.1242/jcs.114.19.3479

Crossref journal-article

The Company of Biologists

Journal of Cell Science (237)

Abstract

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.

Bibliography

Dean, K. A., von Ahsen, O., GoÌrlich, 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), 3479â3485.

Authors 4

Kellie A. Dean (first)
Oliver von Ahsen (additional)
Dirk Görlich (additional)
Howard M. Fried (additional)

References 36 Referenced 49

Dates

Type	When
Created	4 years, 4 months ago (April 25, 2021, 7:39 p.m.)
Deposited	4 years, 4 months ago (April 25, 2021, 7:39 p.m.)
Indexed	5 months, 1 week ago (March 22, 2025, 7:31 a.m.)
Issued	23 years, 11 months ago (Oct. 1, 2001)
Published	23 years, 11 months ago (Oct. 1, 2001)
Published Print	23 years, 11 months ago (Oct. 1, 2001)

Funders 0

None

BibTeX

@article{Dean_2001, title={Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin}, volume={114}, ISSN={0021-9533}, url={http://dx.doi.org/10.1242/jcs.114.19.3479}, DOI={10.1242/jcs.114.19.3479}, number={19}, journal={Journal of Cell Science}, publisher={The Company of Biologists}, author={Dean, Kellie A. and von Ahsen, Oliver and Görlich, Dirk and Fried, Howard M.}, year={2001}, month=oct, pages={3479–3485} }

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  "abstract": "<jats:p>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 \u03b2 superfamily of transport receptors, importin 8 and transportin; SRP19 was also imported less efficiently by several other members of the importin \u03b2 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 \u03b2 family of transport receptors, and the findings add additional evidence for nuclear assembly of SRP.</jats:p>",
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