The engagement of β1 integrins on promonocytic cells promotes phosphorylation of Syk and formation of a protein complex containing Lyn and β1 integrin

Lesley A. Miller, Julie J. Hong, Michael S. Kinch, Marietta L. Harrison, Robert L. Geahlen

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

The protein-tyrosine kinase Syk participates in signal transduction pathways downstream from multiple immune recognition receptors. Recent evidence indicates that Syk is also functionally coupled to cell surface integrins, which mediate interactions between the actin cytoskeleton and extracellular matrix proteins. The interactions of undifferentiated, promonocytic HL60 or U937 cells with fibronectin or anti-β, integrin antibodies leads to an apparent activation and tyrosine phosphorylation of Syk that is independent of tight cellular adhesion and spreading. In response to fibronectin or anti-β1 integrin antibodies, β1 integrins become associated with a complex of proteins that include the Lyn protein tyrosine kinase and endogenous kinase substrates of 29 and 75-80 kDa. Lyn becomes transiently activated following integrin engagement and co-localizes with the actin cytoskeleton. These studies suggest a major role for Lyn in coupling β1 integrins to the activation of Syk.

Original languageEnglish
Pages (from-to)1426-1434
Number of pages9
JournalEuropean Journal of Immunology
Volume29
Issue number5
DOIs
StatePublished - 1999

Keywords

  • Adhesion
  • Integrin
  • Lyn
  • Protein-tyrosine kinase
  • Syk

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