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Article

Role of threonine residues in regulation of the epidermal growth factor receptor by protein kinase C and mitogen-activated protein kinase.

The Journal of biological chemistry - 25 Jul 1993

Morrison P, Takishima K, Rosner M R

Abstract excerpt

Epidermal growth factor (EGF) receptor tyrosine kinase activity is down-regulated by a number of growth-modulating agents that activate protein kinase C and/or mitogen-activated protein (MAP) kinases. Although the mechanism is unclear, it has been hypothesized that phosphorylation of specific threonine residues leads to inhibition of the EGF receptor tyrosine kinase. Two sites phosphorylated on the EGF receptor...

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Source

Identifiers

PMID: 8393447

Genes

EGF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Role of threonine residues in regulation of the epidermal growth factor receptor by protein kinase C and mitogen-activated protein kinase.PMID 8393447Read ↗

Effects of substitution of threonine 654 of the epidermal growth factor receptor on epidermal growth factor-mediated activation of phospholipase C.Semantic proximity Read ↗

Multisite phosphorylation of the epidermal growth factor receptor. Use of site-directed mutagenesis to examine the role of serine/threonine phosphorylation.Semantic proximity Read ↗

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

Constitutive phosphorylation of the epidermal growth factor receptor blocks mitogenic signal transduction.Semantic proximity Read ↗

Mechanism of desensitization of the epidermal growth factor receptor protein-tyrosine kinase.Semantic proximity Read ↗

Regulation of EGF receptor expression and function.Semantic proximity Read ↗

Stimulation of mitogenic pathways through kinase-impaired mutants of the epidermal growth factor receptor.Semantic proximity Read ↗

A variant epidermal growth factor receptor exhibits altered type alpha transforming growth factor binding and transmembrane signaling.Semantic proximity Read ↗

A negative feedback loop attenuates EGF-induced morphological changes.Semantic proximity Read ↗

Multiple autophosphorylation sites of the epidermal growth factor receptor are essential for receptor kinase activity and internalization. Contrasting significance of tyrosine 992 in the native and truncated receptors.Semantic proximity Read ↗

A dominant negative mutation suppresses the function of normal epidermal growth factor receptors by heterodimerization.Semantic proximity Read ↗

Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates.Semantic proximity Read ↗

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