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Assaying Protein Kinase Activity with Radiolabeled ATP

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A highly conserved tyrosine residue at codon 845 within the kinase domain is not required for the transforming

N Gotoh¹, A Tojo, M Hino

¹Department of Genetics, University of Tokyo, Japan.

Biochemical and Biophysical Research Communications

|July 31, 1992

Summary

The tyrosine residue Y845 in epidermal growth factor receptor (EGF-R) is not essential for EGF-R

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Area of Science:

Molecular Biology
Cell Signaling
Biochemistry

Background:

Epidermal growth factor receptor (EGF-R) is a key tyrosine kinase involved in cellular processes.
The Y845 residue in EGF-R is conserved and functionally significant in related kinases.

Purpose of the Study:

To investigate the functional role of the Y845 tyrosine residue in EGF-R signaling.
To determine if Y845 is critical for EGF-R's kinase activity and downstream effects.

Main Methods:

Constructed a mutant human EGF-R with Y845 replaced by phenylalanine (F845).
Transfected NIH3T3 cells with the mutant EGF-R (EGF-R F845).
Assessed EGF-dependent cellular transformation, tyrosine-autophosphorylation, and DNA synthesis.

Main Results:

EGF-R F845 induced EGF-dependent cellular transformation.
The mutant receptor showed tyrosine-autophosphorylation of a 170 kDa protein.
EGF-R F845 initiated DNA synthesis comparable to wild-type EGF-R.

Conclusions:

The Y845 tyrosine residue is dispensable for EGF-R's ability to induce cellular transformation.
Y845 is not required for EGF-R's tyrosine-autophosphorylation or initiation of DNA synthesis.
These findings indicate Y845 is not essential for the studied EGF-R tyrosine kinase functions.