GSBS Student Publications

Title

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

Student Author(s)

Alpna Seth; Ingrid C. Northwood

GSBS Program

Biochemistry & Molecular Pharmacology

UMMS Affiliation

Program in Molecular Medicine; Department of Biochemistry and Molecular Pharmacology

Date

8-15-1991

Document Type

Article

Medical Subject Headings

Amino Acid Sequence; Animals; Chickens; DNA-Binding Proteins; Humans; Mice; Molecular Sequence Data; Peptide Mapping; Phosphorylation; Protein-Tyrosine Kinases; Proto-Oncogene Proteins c-jun; Proto-Oncogene Proteins c-myc; Rats; Receptor, Epidermal Growth Factor; Sequence Alignment; Substrate Specificity; Transcription Factors

Disciplines

Biochemistry, Biophysics, and Structural Biology | Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: J Biol Chem. 1991 Aug 15;266(23):15277-85.

Related Resources

Link to article in PubMed

Journal Title

The Journal of biological chemistry

PubMed ID

1651323