Involvement of cortactin and phosphotyrosine proteins in cell-cell contact formation in cultured bovine corneal endothelial cells

Lily Kredy-Farhan, Shlomo Kotev-Emeth, Naphtali Savion

Research output: Contribution to journalArticlepeer-review

Abstract

Phosphotyrosine proteins involvement, particularly cortactin, was studied in cell-cell contacts of cultured bovine corneal endothelial (BCE) cells. These proteins, including α-catenin, vinculin and cortactin, are localized at cell-cell contacts separate from the cortical actin ring. Approximately 50% of cortactin isoforms p80 and p85 were associated with the Triton-insoluble fraction while phosphotyrosine proteins were in the soluble fraction. Disruption of cell-cell contacts by EDTA treatment was associated with a decrease in cortactin isoforms p80 (26%) and p85 (57%). Cortactin isoform p85 was phosphorylated at Y466, expressed in reattaching cells and associated with the Triton-soluble fraction, whereas cortactin isoform p80 was phosphorylated at Y421 and associated with the Triton-insoluble fraction. In sub-confluent cultures, pY421-cortactin was localized at the leading edge and pY466-cortactin at a perinuclear area. In confluent cultures both pY466- and pY421-cortactin isoforms were localized at the cell-cell contacts. In conclusion, in BCE cells, the most prominent appearance of cortactin was at the cell-cell contacts separate from the cortical actin ring. Isoform p80 was phosphorylated at Y 421 and associated with the Triton-insoluble fraction and isoform p85 was phosphorylated at Y466 and associated with the Triton-insoluble fraction.

Original languageEnglish
Pages (from-to)193-202
Number of pages10
JournalHistochemistry and Cell Biology
Volume129
Issue number2
DOIs
StatePublished - Feb 2008

Keywords

  • Cortactin
  • Cortical actin ring
  • Phospho-cortactin
  • Vinculin
  • α-Catenin

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