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Article

Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.

Molecular and cellular biology - 1 Feb 1990

Margolis B, Bellot F, Honegger A M, Ullrich A, Schlessinger J, Zilberstein A

Abstract excerpt

Epidermal growth factor (EGF) treatment of NIH 3T3 cells transfected with wild-type EGF receptor induced tyrosine phosphorylation of phospholipase C-gamma (PLC-gamma). The EGF receptor and PLC-gamma were found to be physically associated such that antibodies directed against PLC-gamma or the EGF receptor coimmunoprecipitated both proteins. The association between PLC-gamma and wild-type EGF receptor was dependent...

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Source

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Identifiers

PMID: 2153914
DOI: 10.1128/mcb.10.2.435-441.1990
PMCID: PMC360807

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.

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Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.PMID 2153914Read ↗

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The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling.Semantic proximity Read ↗

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Oncogenic forms of the neu/HER2 tyrosine kinase are permanently coupled to phospholipase C gamma.Semantic proximity Read ↗

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

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