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Can Hormones Alter Nuclear Permeability?

The nuclear envelope acts as a barrier to passage between the nucleus and the cytosol. By regulating the envelope's permeability, cells can control the nuclear access of proteins that affect nuclear function, such as transcription factors, kinases, and phosphatases. Nucleocytosolic passage generally occurs through the nuclear pore complex, which restricts movement on the basis of size and the presence of appropriate localization sequences.

GFP moves from cytosol to nucleus in cells stimulated with vasopressin.

In this Paper of the Week, Elizabeth M. O'Brien and colleagues used localized, two-photon activation of a photoactivable green fluorescent protein (GFP) to investigate whether hormones, via their second messengers, could alter nuclear permeability. They found that vasopressin and other hormones that increase cytosolic Ca²⁺ and activate protein kinase C increased permeability across the nuclear membrane. Furthermore, localized photorelease of caged Ca²⁺ near the nuclear envelope resulted in a local increase in nuclear permeability. However, neither activation nor inhibition of protein kinase C affected nuclear permeability. These findings provide evidence that hormones linking to certain G protein-coupled receptors increase nuclear permeability via cytosolic Ca²⁺.

FOOTNOTES

See referenced article, J. Biol. Chem. 2007, 282, 4210-4217

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