| The zinc finger protein ZPR1 (ZNF259) binds to epidermal growth factor receptor (EGFR) and is localized to both cytoplasm and nucleus. The zinc fingers found in ZPR1 and the tyrosine kinase domain of EGFR mediate the interaction between ZPR1 and the receptor. ZPR1 translocates from the cytoplasm to nucleus following mitogen (i.e. EGF) stimulation. ZPR1 also interacts with translation elongation factor eEF1A in vivo following EGF treatment. The interaction between the zinc finger protein and elongation factor is important for cell proliferation. Cells lacking ZPR1 exhibit abnormal nucleolar function, suggesting that ZPR1 is required for cell viability and nucleolar function in dividing cells. ZPR1 knockout mice exhibit significant neurodegeneration, and reduced or altered expression of ZPR1 may contribute to spinal muscular atrophy, a disorder characterized by degeneration of spinal cord neurons. |
