Cutting edge: a novel function for the SLAP-130/FYB adapter protein in β1 integrin signaling and T lymphocyte migration

AJ Hunter, N Ottoson, N Boerth… - The Journal of …, 2000 - journals.aai.org
AJ Hunter, N Ottoson, N Boerth, GA Koretzky, Y Shimizu
The Journal of Immunology, 2000journals.aai.org
The role of integrin-mediated signaling events in T cell function remains incompletely
characterized. We report here that α 4 β 1 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 α 4 β 1 integrin enhances the association of tyrosine …
Abstract
The role of integrin-mediated signaling events in T cell function remains incompletely characterized. We report here that α 4 β 1 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 α 4 β 1 integrin enhances the association of tyrosine phosphorylated SLAP-130/FYB with the SH2 domain of the src tyrosine kinase p59 fyn. Activation of normal T cells, but not H9 T cells, via α 4 β 1 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)-1α. These results identify SLAP-130/FYB as a new tyrosine phosphorylated substrate in β 1 integrin signaling and suggest a novel function for SLAP-130/FYB in regulating T lymphocyte motility.
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