Blog
About

  • Record: found
  • Abstract: found
  • Article: not found

Ser756 of β2 integrin controls Rap1 activity during inside-out activation of αMβ2.

Biochemical Journal

metabolism, rap1 GTP-Binding Proteins, pharmacology, Tetradecanoylphorbol Acetate, Talin, Sheep, chemistry, Serine, Mutation, drug effects, Macrophages, Macrophage-1 Antigen, Humans, Gene Expression Regulation, Erythrocytes, Cercopithecus aethiops, COS Cells, Antigens, CD18, Antibodies, Animals

Read this article at

ScienceOpenPublisherPubMed
Bookmark
      There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

      Abstract

      During αMβ2-mediated phagocytosis, the small GTPase Rap1 activates the β2 integrin by binding to a region between residues 732 and 761. Using COS-7 cells transfected with αMβ2, we show that αMβ2 activation by the phorbol ester PMA involves Ser(756) of β2. This residue is critical for the local positioning of talin and biochemically interacts with Rap1. Using the CaM (calmodulin) antagonist W7, we found Rap1 recruitment and the inside-out activation of αMβ2 to be affected. We also report a role for CaMKII (calcium/CaM-dependent kinase II) in the activation of Rap1 during integrin activation. These results demonstrate a distinct physiological role for Ser(756) of β2 integrin, in conjunction with the actions of talin and Rap1, during αMβ2 activation in macrophages. © The Authors Journal compilation © 2011 Biochemical Society

      Related collections

      Author and article information

      Journal
      10.1042/BJ20101666
      21605078

      Comments

      Comment on this article