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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Unique motif for nucleolar retention and nuclear export regulated by phosphorylation.

By microinjecting purified glutathione S-transferase linked to all or parts of herpes simplex virus type 1 US11 protein into either the nucleus or the cytoplasm, we have demonstrated that this nucleolar protein exhibits a new type of localization signal controlling both retention in nucleoli and export to the cytoplasm. Saturated mutagenesis combined with computer modeling allowed us to draw the fine-structure map of this domain, revealing a new proline-rich motif harboring both activities, which are temperature dependent and regulated by phosphorylation. Finally, crossing the nuclear pore complex from the cytoplasm to the nucleus is an energy-dependent process for US11 protein, while getting to nucleoli through the nucleoplasm is energy independent.[1]

References

  1. Unique motif for nucleolar retention and nuclear export regulated by phosphorylation. Catez, F., Erard, M., Schaerer-Uthurralt, N., Kindbeiter, K., Madjar, J.J., Diaz, J.J. Mol. Cell. Biol. (2002) [Pubmed]
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