Expression and tyrosine phosphorylation of Cbl regulates macrophage chemokinetic and chemotactic movement

Elena Caveggion, Silvia Continolo, Fiona J. Pixley, E. Richard Stanley, David D.L. Bowtell, Clifford A. Lowell, Giorgio Berton

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


Primary macrophages isolated from hck-/-fgr-/- mice display altered morphology and F-actin cytoskeletal structures and reduced migration. The ability of phorbol myristyl acetate (PMA), a protein kinase C activator that has been reported to increase macrophage spreading and carcinoma cell motility, to rescue these hck-/- fgr-/- defects was tested. Although PMA-treated wild-type and hck-/-fgr-/- macrophages exhibited a similar flattened, spread phenotype, PMA did not rescue the hck-/-fgr-/- macrophage migration defect. Instead, both PMA-treated wild type and hck-/-fgr-/- macrophages were defective in spontaneous and chemotactic migration and tyrosine phosphorylation of the Cbl protooncoprotein was decreased in both. Moreover, c-cbl-/- macrophages displayed the same impairment of motility as hck-/-fgr-/- macrophages and a similar morphology with less polarization and more dorsal ruffling than wild-type macrophages. As Hck and Fgr expression and activity were not decreased in c-cbl-/- macrophages, these results suggest that Cbl is likely to be an important downstream mediator of the Src family kinase-regulated macrophage motility pathway.

Original languageEnglish (US)
Pages (from-to)276-289
Number of pages14
JournalJournal of Cellular Physiology
Issue number2
StatePublished - May 1 2003

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology


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