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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
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Integrin CD11c/CD18 α-chain phosphorylation is functionally important

Liisa M Uotila1, Maria Aatonen, Carl G Gahmberg

  • 1From the Division of Biochemistry and Biotechnology, Department of Biosciences, University of Helsinki, 00014 Helsinki, Finland.

The Journal of Biological Chemistry
|October 17, 2013
PubMed

CD11c/CD18 (αXβ2, p150/95, or complement receptor 4, CR4) is a monocyte/macrophage-enriched integrin that has been reported to bind to a variety of ligands. These include cell surface proteins, extracellular matrix proteins, and soluble ligands. The regulation of ligand binding to CD11c/CD18 has remained poorly understood. Previous work has shown that both α-chain and β-chain phosphorylations of CD11a/CD18 and CD11b/CD18 are needed for activity, but no corresponding studies on CD11c/CD18 have been performed. In this study, we have identified the phosphorylation site of CD11c as Ser-1158 and show that it is pivotal for adherence and phagocytosis.

Keywords:
AdhesionIntegrinsLeukocytePhagocytosisPhosphorylation

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