Presence of oxidized cholesterol in caveolae uncouples active platelet-derived growth factor receptors from tyrosine kinase substrates

P. Liu, P. Y. Wang, P. Michaely, M. Zhu, R. G W Anderson

Research output: Contribution to journalArticle

46 Scopus citations

Abstract

Platelet-derived growth factor receptor β (PDGFRβ) in fibroblasts is concentrated in caveolae where it controls the tyrosine phosphorylation of multiple proteins. Caveolae are enriched in cholesterol and sphingolipids, but the role of these lipids in PDGFR signal transduction is unknown. We report that introduction of cholest-4-en-3-one into caveolae membranes uncouples PDGFR autophosphorylation from tyrosine phosphorylation of neighboring proteins. Cholest-4-en-3-one appears to interfere with the normal interaction between PDGFR and its partners. The results suggest that tightly packed caveolae lipids form a membrane platform that functions as a lipid scaffold for organizing the molecular interactions of multiple signaling pathways.

Original languageEnglish (US)
Pages (from-to)31648-31654
Number of pages7
JournalJournal of Biological Chemistry
Volume275
Issue number41
DOIs
StatePublished - Oct 13 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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