Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase
A growth factor-stimulated (MAP2-related) protein kinase, ERT, that phosphorylates the epidermal growth factor receptor at Thr669 has been purified from KB human tumor cells by Northwood and co-workers (Northwood, I. C., Gonzalez, F. A., Wartmann, M., Raden, D. L., and Davis, R. J. (1991) J. Biol. C...
Saved in:
Published in: | The Journal of biological chemistry 1991-08, Vol.266 (23), p.15277-15285 |
---|---|
Main Authors: | , , , , , , , |
Format: | Article |
Language: | eng |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Summary: | A growth factor-stimulated (MAP2-related) protein kinase, ERT, that phosphorylates the epidermal growth factor receptor at
Thr669 has been purified from KB human tumor cells by Northwood and co-workers (Northwood, I. C., Gonzalez, F. A., Wartmann,
M., Raden, D. L., and Davis, R. J. (1991) J. Biol. Chem. 266, 15266-15276). The ERT protein kinase has a restricted substrate
specificity, and the structural determinants employed for substrate recognition by this enzyme have not been defined. As an
approach toward understanding the specificity of substrate phosphorylation, we have used an in vitro assay to identify additional
substrates for the ERT protein kinase. In this report we describe two novel substrates: (a) the human c-myc protein at Ser62
and (b) the rat c-jun protein at Ser246. Alignment of the primary sequences surrounding the phosphorylation sites located
within the epidermal growth factor receptor (Thr669), Myc (Ser62), and Jun (Ser246) demonstrated a marked similarity. The
observed consensus sequence was Pro-Leu-Ser/Thr-Pro. We propose that this sequence forms part of a substrate structure that
is recognized by the ERT protein kinase. |
---|---|
ISSN: | 0021-9258 1083-351X |