Integrin CD11c/CD18 α-chain phosphorylation is functionally important
| Autor: | Carl G. Gahmberg, Maria Aatonen, Liisa M. Uotila |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
Integrin
chemical and pharmacologic phenomena CD18 Complement receptor Biochemistry 03 medical and health sciences 0302 clinical medicine Phagocytosis Chlorocebus aethiops Cell Adhesion Animals Humans Phosphorylation Receptor Cell adhesion Molecular Biology 030304 developmental biology 0303 health sciences COS cells integumentary system biology Chemistry hemic and immune systems Cell Biology 3. Good health Cell biology CD11c Antigen Integrin alpha M CD18 Antigens COS Cells biology.protein K562 Cells 030215 immunology Reports |
| Zdroj: | The Journal of biological chemistry. 288(46) |
| ISSN: | 1083-351X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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