Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Carrier Proteins / chemistry
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Carrier Proteins / metabolism*
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Cell Line
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Cell Nucleus / metabolism
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Cloning, Molecular
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Cytoplasm / metabolism
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Epidermal Growth Factor / pharmacology
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ErbB Receptors / chemistry
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ErbB Receptors / metabolism*
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Humans
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Immunoblotting
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Intracellular Signaling Peptides and Proteins
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Male
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Membrane Transport Proteins
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Mice
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Molecular Sequence Data
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Phosphorylation
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Phosphotyrosine / metabolism
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Protein Structure, Secondary
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RNA, Messenger / genetics
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RNA, Messenger / metabolism
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Testis / metabolism
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Type C Phospholipases / metabolism
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Vanadates / pharmacology
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Zinc Fingers*
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src Homology Domains
Substances
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Carrier Proteins
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Intracellular Signaling Peptides and Proteins
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Membrane Transport Proteins
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RNA, Messenger
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ZPR1 protein, human
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Zfp259 protein, mouse
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Phosphotyrosine
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Vanadates
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Epidermal Growth Factor
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ErbB Receptors
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Type C Phospholipases