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Science 21 June 1996:
Vol. 272. no. 5269, pp. 1717 - 0
DOI:

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When activated, the epidermal growth factor (EGF) becomes phosphorylated on tyrosine residues. Proteins that participate in signal transduction within a cell then bind to the receptor at these phosphorylation sites. Galcheva-Gargova et al. (p. 1797) now describe a protein that interacts in an opposite way with the EGF receptor. The protein, called ZPR1, binds to the inactive receptor and is released after binding of EGF. ZPR1 then becomes localized in the nucleus in cells treated with EGF. These properties, and the fact that it contains two zinc fingers found in other proteins that function in receptor signaling, indicate that ZPR1 may participate in transmission of signals from the EGF receptor at the cell surface to the nucleus.




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