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• W2083375615 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." @default.
• W2083375615 created "2016-06-24" @default.
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• W2083375615 date "2009-07-28" @default.
• W2083375615 modified "2023-10-11" @default.
• W2083375615 title "SLP-76-ADAP adaptor module regulates LFA-1 mediated costimulation and T cell motility" @default.
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• W2083375615 doi "https://doi.org/10.1073/pnas.0900510106" @default.
• W2083375615 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2710989" @default.
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• W2083375615 hasPublicationYear "2009" @default.
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