Structure, Function and Nucleocytoplasmatic Traffic of Nuclear Proteins

Structure, Function and Nucleocytoplasmatic Traffic of Nuclear Proteins

Nuclear chaperones are involved among other functions in the chromatin remodeling that take place during various physiological processes such as fertilization (e.g. mediated by nucleoplasmin) and ribosome assembly and cell proliferation control (e.g. mediated by nucleophosmin). Like other nuclear proteins, they are synthesized in the cytoplasm and rely on carriers (in the case of nucleoplasmin / nucleophosmin family, importin α/β heterodimer carrier) to be imported into the cell nucleus. Nucleophosmin is a “shuttling” protein: it needs to be imported and exported continuously. Protein function is frequently regulated by cell localization, and failure in this traffic may trigger diseases. Nucleophosmin mislocalization and disfunction have been related to several types of human cancer. This research line focuses on nucleophosmin structure, function and interaction with nuclear transport receptors, trying to understand the basis of its pathogenic alterations.

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