4.6 Article

Integrin CD11c/CD18 α-Chain Phosphorylation Is Functionally Important

期刊

JOURNAL OF BIOLOGICAL CHEMISTRY
卷 288, 期 46, 页码 33494-33499

出版社

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C113.497446

关键词

Adhesion; Integrins; Leukocyte; Phagocytosis; Phosphorylation

资金

  1. Academy of Finland
  2. Sigrid Juselius Foundation
  3. Finska Lakaresallskapet
  4. Liv och Halsa Foundation
  5. Magnus Ehrnrooth Foundation
  6. Wilhelm and Else Stockmann Foundation

向作者/读者索取更多资源

CD11c/CD18 ((X2), 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 -chain and -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.

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