Role of dimerization and modification of the CSF-1 receptor in its activation and internalization during the CSF-1 response

W. Li, E. R. Stanley

Research output: Contribution to journalArticle

106 Scopus citations


We have used kinetic and cross-linking approaches to study CSF-I-induced changes in the structure and function of the CSF-1R. Addition of CSF-1 to cells stimulates or stabilizes non-covalent CSF-1R dimerization resulting inactivation of the CSF-1R kinase and the tyrosine phosphorylation of the receptor and certain cytoplasmic proteins. The non-covalent dimers become covalently linked via disulfide bonds and/or are subsequently further modified. These modified forms are selectively internalized. Pre-treatment of cells with the alkylating agent, iodoacetic acid (IAA), selectively inhibits covalent dimerization, modification and internalization but enhances protein tyrosine phosphorylation. It is proposed that ligand-induced non-covalent dimerization activates the CSF-1R kinase, whereas the covalent dimerization and subsequent modification lead to kinase inactivation, phosphotyrosine dephosphorylation and internalization of the receptor-ligand complex.

Original languageEnglish (US)
Pages (from-to)277-288
Number of pages12
JournalEMBO Journal
Issue number2
Publication statusPublished - Feb 20 1991



  • CSF-1
  • growth factor receptor
  • receptor internalization
  • signal transduction
  • tyrosine phosphorylation

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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