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Article Dans Une Revue Molecular and Cellular Biology Année : 2002

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

Résumé

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.
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Dates et versions

hal-00180265 , version 1 (18-10-2007)

Identifiants

  • HAL Id : hal-00180265 , version 1
  • PUBMED : 11809804

Citer

Frédéric Catez, Monique Erard, Nathalie Schaerer-Uthurralt, Karine Kindbeiter, Jean-Jacques Madjar, et al.. Unique motif for nucleolar retention and nuclear export regulated by phosphorylation.. Molecular and Cellular Biology, 2002, 22 (4), pp.1126-39. ⟨hal-00180265⟩
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