Phosphorylation of insulin-like growth factor binding protein-3 by deoxyribonucleic acid-dependent protein kinase reduces ligand binding and enhances nuclear accumulation.

@article{Schedlich2003PhosphorylationOI,
  title={Phosphorylation of insulin-like growth factor binding protein-3 by deoxyribonucleic acid-dependent protein kinase reduces ligand binding and enhances nuclear accumulation.},
  author={Lynette J Schedlich and Trine Nilsen and Anna P John and David Andrew Jans and Robert C. Baxter},
  journal={Endocrinology},
  year={2003},
  volume={144 5},
  pages={1984-93}
}
The IGF binding proteins (IGFBPs) regulate the mitogenic effects of IGFs in the extracellular environment. Several members of this family, including IGFBP-3, also appear to have IGF-independent effects on cell function. For IGFBP-3 and IGFBP-5, both of which are translocated to the cell nuclei, these effects may be related to their putative nuclear actions. Because reversible phosphorylation is an important mechanism for controlling nuclear protein import, we have examined the effect of… CONTINUE READING
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