Cell Adhesion Molecule CEACAM1 Associates with Paxillin in Granulocytes and Epithelial and Endothelial Cells
作者： A. Ebrahimnejad , R. Flayeh , G. Unteregger , C. Wagener , J. Brümmer
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摘要: Abstract CEACAM1 functions as an epithelial tumor suppressor and angiogenic growth factor. In the present study, utilizing differentially (serine/threonine or tyrosine) phosphorylated cytoplasmic domains of CEACAM3 bait to isolate associated proteins from granulocyte extracts, we have identified human paxillin a binding partner tyrosine-phosphorylated domain. CEACAM1–paxillin complexes were coimmunoprecipitated extracts granulocytes, colonic cell line HT29, HUVECs. We Tyr-488—a residue in domain known be essential for suppressive effect—to necessary this association. The interaction was confirmed using laser scanning confocal microscopy analyses granulocytes HT29 cells, where colocalizes with at plasma membrane. HUVECs highly polarized expression pattern colocalization observed. These findings support that is linked actin-based cytoskeleton.
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