PDGF beta-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex.

doi:10.1016/0092-8674(90)90220-9

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Article

PDGF beta-receptor stimulates tyrosine phosphorylation of GAP and association of GAP with a signaling complex.

Cell - 6 Apr 1990

Kaplan D R, Morrison D K, Wong G, McCormick F, Williams L T

Abstract excerpt

Platelet-derived growth factor (PDGF) stimulated the tyrosine phosphorylation of the GTPase activating protein (GAP) in 3T3 cells and in CHO cells expressing wild-type PDGF receptors, but not in several CHO cell lines expressing mutant receptors defective in transmitting mitogenic signals. Following PDGF treatment of cells, GAP physically associated with the PDGF receptor and with Raf-1, phospholipase c-gamma,...

Topics

Animals
Cell Line
Cell Transformation, Neoplastic
Cells, Cultured
GTPase-Activating Proteins
Genes, ras
Macromolecular Substances
Mice
Mutation
Phosphorylation
Platelet-Derived Growth Factor

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Kinases

Proteins

Receptors, Cell Surface

Receptors, Platelet-Derived Growth Factor

Signal Transduction

Tyrosine

ras GTPase-Activating Proteins

Source

Open in PubMed

Identifiers

PMID: 2156626
DOI: 10.1016/0092-8674(90)90220-9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2156626-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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