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Nuclear import of SRP proteins: In eukaryotic cells, SRP mediates translocation of nascent
polypeptides from the ribosome into the endoplasmic reticulum.
Since SRP functions in the cytoplasm but contains an RNA molecule,
a mechanism must exist for SRP RNA to be exported from the nucleus.
We were the first to provide evidence that SRP RNA partly
assembles with SRP proteins in the nucleus as a prerequisite for
export to the cytoplasm. Recently, genetic
analysis in yeast and immunolocalization studies with mammalian cells has confirmed that most SRP proteins are located to
some extent in the nucleus and nucleolus (see Figure 1). Further, we found that human SRP19 can be imported into the nucleus by either of two nuclear transport factors, transportin and importin 8. Transportin is a well characterized member of the importin β family of nuclear transport factors;, importin 8 was only suspected to be an nuclear import factor until we confirmed its function (Figure 2). |
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| Figure 1. SRP19 colocalizes with fibrillarin, a nucleolar protein. Left: HeLa cells stained with antibody to fibrillarin. Middle: Cells stained with SRP19 antibody. Right: Merged image. Modified from Dean, K. et al., J. Cell Sci. 114: 3479, 2001. © The Company of Biologists, Ltd.
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