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A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming activity of human epidermal growth factor receptor.

Authors
  • Gotoh, N
  • Tojo, A
  • Hino, M
  • Yazaki, Y
  • Shibuya, M
Type
Published Article
Journal
Biochemical and biophysical research communications
Publication Date
Jul 31, 1992
Volume
186
Issue
2
Pages
768–774
Identifiers
PMID: 1323290
Source
Medline
License
Unknown

Abstract

Epidermal growth factor receptor (EGF-R) is a widely expressed ligand-dependent tyrosine kinase. The tyrosine residue at 845 in EGF-R corresponds to Y416 of v/c-src kinase, which is highly conserved and functionally important in many tyrosine kinases. To clarify the functional role of Y845, we constructed a mutant human EGF-R in which this tyrosine was replaced with phenylalanine and transfected it to NIH3T3 cells. EGF-R F845 induced EGF-dependent cellular transformation and revealed tyrosine-autophosphorylation of a 170 kDa protein, and initiated DNA synthesis similar to the wild-type EGF-R. We conclude here that Y845 is dispensable in the above mentioned functions of EGF-R tyrosine kinase.

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