Mutational removal of the Thr669 and Ser671 phosphorylation sites alters substrate specificity and ligand-induced internalization of the epidermal growth factor receptor.

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Article

Mutational removal of the Thr669 and Ser671 phosphorylation sites alters substrate specificity and ligand-induced internalization of the epidermal growth factor receptor.

The Journal of biological chemistry - 5 Aug 1990

Heisermann G J, Wiley H S, Walsh B J, Ingraham H A, Fiol C J, Gill G N

Abstract excerpt

The epidermal growth factor (EGF) receptor contains multiple sites of phosphorylation on serine, threonine, and tyrosine residues. Because the biological responsiveness of the EGF receptor is regulated by phosphorylation at several of these sites, we studied the functional consequences of removal of the Thr669 and Ser671 phosphorylation sites using site-directed mutagenesis. The mutant EGF receptor expressed in...

Topics

Amino Acid Sequence
Animals
Base Sequence
Casein Kinases
Cell Line
Endocytosis
Epidermal Growth Factor
ErbB Receptors
Kinetics
Ligands
Mice

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Oligonucleotide Probes

Oligopeptides

Phosphorylation

Protein Kinases

Restriction Mapping

Source

Open in PubMed

Identifiers

PMID: 2115882

Genes

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2115882-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Mutational removal of the Thr669 and Ser671 phosphorylation sites alters substrate specificity and ligand-induced internalization of the epidermal growth factor receptor.PMID 2115882Read ↗

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