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CUTTING EDGE |
*
Department of Laboratory Medicine and Pathology, Center for Immunology, Cancer Center, University of Minnesota Medical School, Minneapolis, MN 55455; and
Department of Pathology and Lab Medicine, Leonard and Madlyn Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, PA 19104
The role of integrin-mediated signaling events in T cell
function remains incompletely characterized. We report here that
4ß1 integrin stimulation of H9 T cells and
normal human T cell blasts results in rapid and transient tyrosine
phosphorylation of the adapter protein, SH2
domain-containing 76-kDa protein (SLP-76)-associated phosphoprotein of
130 kDa (SLAP-130)/FYB at levels comparable to those observed following
TCR stimulation. Stimulation of T cells via the
4ß1 integrin enhances the association of
tyrosine phosphorylated SLAP-130/FYB with the SH2 domain of
the src tyrosine kinase p59fyn.
Activation of normal T cells, but not H9 T cells, via
4ß1 leads to tyrosine
phosphorylation of SLP-76 as well as SLAP-130/FYB.
Overexpression of SLAP-130/FYB in normal T cells enhances T cell
migration through fibronectin-coated filters in response to the
chemokine stromal cell-derived factor (SDF)-1. These results
identify SLAP-130/FYB as a new tyrosine phosphorylated
substrate in ß1 integrin signaling and suggest a novel
function for SLAP-130/FYB in regulating T lymphocyte
motility.
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