SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility

Proc Natl Acad Sci U S A. 2009 Jul 28;106(30):12436-41. doi: 10.1073/pnas.0900510106. Epub 2009 Jul 15.

Abstract

Although adaptor ADAP (FYB) and its binding to SLP-76 has been implicated in TcR-induced "inside-out" signaling for LFA-1 activation in T cells, little is known regarding its role in LFA-1-mediated "outside-in" signaling. In this study, we demonstrate that ADAP and SLP-76-ADAP binding are coupled to LFA-1 costimulation of IL-2 production, F-actin clustering, cell polarization, and T cell motility. LFA-1 enhancement of anti-CD3-induced IL-2 production was completely dependent on SLP-76-ADAP binding. Further, anti-CD3 was found to require CD11a ligation by antibody or ICAM1 to cause T cell polarization. ADAP augmented this polarization induced by anti-CD3/CD11a, but not by anti-CD3 alone. ADAP expression with LFA-1 ligation alone was sufficient to polarize T cells directly and to increase T cell motility whereas the loss of ADAP in ADAP-/- primary T cells reduced motility. A mutant lacking SLP-76-binding sites (M12) blocked LFA-1 costimulation of IL-2 production, polarization, and motility. LFA-1-ADAP polarization was also dependent on src kinases, Rho GTPases, phospholipase C, and phosphoinositol 3-kinase. Our findings provide evidence of an obligatory role for the SLP-76-ADAP module in LFA-1-mediated costimulation in T cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Adaptor Proteins, Signal Transducing / genetics
  • Adaptor Proteins, Signal Transducing / metabolism*
  • Animals
  • Antibodies / pharmacology
  • Binding Sites
  • CD3 Complex / immunology
  • Cell Line
  • Cell Movement / drug effects
  • Cell Polarity / drug effects
  • Cells, Cultured
  • Chromones / pharmacology
  • Enzyme Inhibitors / pharmacology
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • Intercellular Adhesion Molecule-1 / pharmacology
  • Interleukin-2 / metabolism
  • Lymphocyte Function-Associated Antigen-1 / metabolism
  • Mice
  • Morpholines / pharmacology
  • Mutation
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphoinositide-3 Kinase Inhibitors
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Pyrimidines / pharmacology
  • Signal Transduction / drug effects
  • T-Lymphocytes / cytology
  • T-Lymphocytes / drug effects
  • T-Lymphocytes / metabolism
  • rho GTP-Binding Proteins / antagonists & inhibitors
  • rho GTP-Binding Proteins / metabolism
  • src-Family Kinases / antagonists & inhibitors
  • src-Family Kinases / metabolism

Substances

  • AG 1879
  • Actins
  • Adaptor Proteins, Signal Transducing
  • Antibodies
  • CD3 Complex
  • Chromones
  • Enzyme Inhibitors
  • Fyb protein, mouse
  • Interleukin-2
  • Lymphocyte Function-Associated Antigen-1
  • Morpholines
  • Phosphoinositide-3 Kinase Inhibitors
  • Phosphoproteins
  • Pyrimidines
  • SLP-76 signal Transducing adaptor proteins
  • Intercellular Adhesion Molecule-1
  • Green Fluorescent Proteins
  • 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one
  • src-Family Kinases
  • rho GTP-Binding Proteins