Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis.

doi:10.1038/358678a0

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Article

Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis.

Nature - 20 Aug 1992

Peters K G, Marie J, Wilson E, Ives H E, Escobedo J, Del Rosario M, Mirda D, Williams L T

Abstract excerpt

Stimulation of certain receptor tyrosine kinases results in the tyrosine phosphorylation and activation of phospholipase C gamma (PLC gamma), an enzyme that catalyses the hydrolysis of phosphatidylinositol (PtdIns). This hydrolysis generates diacylglycerol and free inositol phosphate, which in turn activate protein kinase C and increase intracellular Ca2+, respectively. PLC gamma physically associates with...

Topics

Amino Acid Sequence
Animals
Base Sequence
Calcium
Fibroblast Growth Factors
In Vitro Techniques
Mitosis
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Oligodeoxyribonucleotides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptides

Phosphatidylinositols

Phosphorylation

Phosphotyrosine

Protein-Tyrosine Kinases

Rats

Receptors, Cell Surface

Source

Open in PubMed

Identifiers

PMID: 1379697
DOI: 10.1038/358678a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1379697-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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