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Science 21 June 1996:
Vol. 272. no. 5269, pp. 1797 - 1802
DOI: 10.1126/science.272.5269.1797
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Reports

Binding of Zinc Finger Protein ZPR1 to the Epidermal Growth Factor Receptor

Zoya Galcheva-Gargova, Konstantin N. Konstantinov, I-Huan Wu, F. George Klier, Tamera Barrett, Roger J. Davis *

ZPR1 is a zinc finger protein that binds to the cytoplasmic tyrosine kinase domain of the epidermal growth factor receptor (EGFR). Deletion analysis demonstrated that this binding interaction is mediated by the zinc fingers of ZPR1 and subdomains X and XI of the EGFR tyrosine kinase. Treatment of mammalian cells with EGF caused decreased binding of ZPR1 to the EGFR and the accumulation of ZPR1 in the nucleus. The effect of EGF to regulate ZPR1 binding is dependent on tyrosine phosphorylation of the EGFR. ZPR1 therefore represents a prototype for a class of molecule that binds to the EGFR and is released from the receptor after activation.

Z. Galcheva-Gargova, I-H. Wu, T. Barrett, R. J. Davis, Program in Molecular Medicine, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School and Howard Hughes Medical Institute, Worcester, MA 01605, USA.
K. N. Konstantinov and F. G. Klier, Department of Molecular and Experimental Medicine, and Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037, USA.
* To whom correspondence should be addressed.


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