Analysis of dynamic tyrosine phosphoproteome in LFA-1 triggered migrating T-cells.
FREELEY, MICHAEL GERARD
VERMA, NAVIN KUMAR
KELLEHER, DERMOT P
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Citation:Verma NK, Dempsey E, Freeley M, Botting CH, Long A, Kelleher D, Volkov Y, Analysis of dynamic tyrosine phosphoproteome in LFA-1 triggered migrating T-cells., Journal of Cellular Physiology, 226, 6, 2011, 1489 1498
The ordered, directional migration of T-lymphocytes is a key process during immune surveillance and response. This requires cell adhesion to the high endothelial venules or to the extracellular matrix by a series of surface receptor/ligand interactions involving adhesion molecules of the integrin family including lymphocyte function associated molecule-1 (LFA-1) and intercellular adhesion molecules (ICAMs). Reversible protein phosphorylation is emerging as a key player in the regulation of biological functions with tyrosine phosphorylation playing a crucial role in signal transduction. Thus, the study of this type of post-translational modification at the proteomic level has great biological significance. In this work, phospho-enriched cell lysates from LFA-1-triggered migrating human T-cells were subjected to immunoaffinity purification of tyrosine phosphorylated proteins, mass spectrometric, and bioinformatic analysis. In addition to the identification of several well-documented proteins, the analysis suggested involvement of a number of new and novel proteins in LFA-1 induced T-cell migration. This dataset expands the list of the signaling components of the LFA-1 induced phosphotyrosine protein complexes in migrating T-cells that will be extremely useful in the study of their specific roles within LFA-1 associated signaling pathways. Identification of proteins previously not reported in the context of LFA-1 stimulated signal transduction might provide new insights into understanding the LFA-1 signaling networks and aid in the search for new potential therapeutic targets.
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Higher Education Authority
Series/Report no:Journal of Cellular Physiology