Publication Date:
1996-06-21
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Galcheva-Gargova, Z -- Konstantinov, K N -- Wu, I H -- Klier, F G -- Barrett, T -- Davis, R J -- R01-CA58396/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1996 Jun 21;272(5269):1797-802.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester, 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8650580" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
Carrier Proteins/chemistry/*metabolism/secretion
;
Cell Line
;
Cell Nucleus/metabolism
;
Cloning, Molecular
;
Cytoplasm/metabolism
;
Epidermal Growth Factor/pharmacology
;
Humans
;
Immunoblotting
;
Male
;
Mice
;
Molecular Sequence Data
;
Phosphorylation
;
Phosphotyrosine/metabolism
;
Protein Structure, Secondary
;
RNA, Messenger/genetics/metabolism
;
Receptor, Epidermal Growth Factor/chemistry/*metabolism
;
Testis/metabolism
;
Type C Phospholipases/metabolism
;
Vanadates/pharmacology
;
*Zinc Fingers
;
src Homology Domains
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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