The kinase insert domain of colony stimulating factor-1 receptor is dispensable for CSF-1 induced phosphatidylcholine hydrolysis

Goutam Ghosh Choudhury, Victor L. Sylvia, Ling Mei Wang, Jacalyne Pierce, Alan Y. Sakaguchi

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Mouse NIH 3T3 fibroblasts transfected with human colony stimulating factor-1 receptor produced diacylglycerol in response to CSFI and this correlated with elevated phosphatidylcholine hydrolyzing activity measured in an in vitro assay. Treatment of cells with the isoflavone derivative genistein attenuated PC hydrolysis in vitro suggesting a role for CSF1R tyrosine kinase activity. A CSF1R mutant lacking 67 amino acids of the kinase insert domain, which may affect the association of receptor with certain substrates, stimulated PC hydrolysis in response to CSF1. Coupling to PC hydrolysis is likely a general property of CSFIR and the kinase insert domain is dispensable for this activity.

Original languageEnglish (US)
Pages (from-to)351-354
Number of pages4
JournalFEBS Letters
Volume282
Issue number2
DOIs
StatePublished - May 6 1991

Keywords

  • Colony stimulating factor-1 receptor
  • NIH 3T3 cell
  • Phosphatidylcholine hydrolysis
  • Tyrosine kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'The kinase insert domain of colony stimulating factor-1 receptor is dispensable for CSF-1 induced phosphatidylcholine hydrolysis'. Together they form a unique fingerprint.

Cite this