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Significance We performed a screen to identify unique proteins regulating T-cell adhesion downstream of the chemokine receptor CXCR4. We identified that the guanine exchange factor mediating stromal cell-derived factor 1 alpha (SDF-1α)/C-X-C chemokine receptor type 4 (CXCR4) activation is phospholipase Cε 1 (PLCε1). Experiments to separate the dual-enzymatic function of PLCε1 uncover necessary contributions of the CDC25, Pleckstrin homology, and Ras-associating domains, but not phospholipase activity, to its guanine exchange activity. In the mouse model of contact sensitivity, we have shown a necessary role for PLCε1 in T-cell recruitment to the site of secondary challenge, but not for priming after antigen sensitization. We uncover a signaling pathway that mediates SDF-1α–induced T-cell adhesion and suggest that PLCε1 is a potential specific target for future antiinflammatory drugs.

PLCε1 regulates SDF-1α–induced lymphocyte adhesion and migration to sites of inflammation