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Updated: May 6, 2026
09:14
Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes
Published on: June 13, 2014
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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
Summary
Researchers identified a key phosphorylation site, Ser-1158, on CD11c integrin. This finding is crucial for understanding how CD11c/CD18 regulates monocyte and macrophage adherence and phagocytosis.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- CD11c/CD18, also known as complement receptor 4 (CR4), is an integrin found on monocytes and macrophages.
- This integrin plays a role in binding various ligands, but the regulation of its function is not well understood.
- Previous studies highlighted the importance of integrin phosphorylation for CD11a/CD18 and CD11b/CD18 activity, but CD11c/CD18 remained unstudied.
Purpose of the Study:
- To investigate the phosphorylation of the CD11c integrin subunit.
- To determine the functional significance of CD11c phosphorylation in cellular processes.
Main Methods:
- Phosphorylation site analysis of the CD11c integrin.
- Functional assays measuring adherence and phagocytosis.
Main Results:
- The phosphorylation site on CD11c was identified as Ser-1158.
- Phosphorylation at Ser-1158 was found to be critical for CD11c/CD18-mediated adherence.
- This phosphorylation event is also pivotal for phagocytosis mediated by CD11c/CD18.
Conclusions:
- Serine 1158 is a key regulatory phosphorylation site on CD11c.
- Understanding CD11c phosphorylation provides insights into monocyte/macrophage function.
- This discovery opens new avenues for targeting CD11c/CD18 in immune responses.
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