Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1).

By Kyle J. Garton, P. Gough, C. Blobel, G. Murphy, D. Greaves, P. Dempsey, E. Raines. Journal of Biological Chemistry, 2001

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ERK-mediated phosphorylation of Thr735 in TNFα-converting enzyme and its potential role in TACE protein trafficking (2005, background): “, 2000), fractalkine (Garton et al., 2001) and β-amyloid precursor protein (Slack et al.”
The ADAMs family of metalloproteases: multidomain proteins with multiple functions. (2003, background): “ADAM17 null cells fail to shed fractalkine in response to a TPA stimulus (Garton et al. 2001), suggesting that ADAM17 is the responsible enzyme.”
Metalloprotease‐disintegrin ADAM8: Expression analysis and targeted deletion in mice (2005, background): “…several ligands of the EGF receptor (Peschon et al., 1998; Merlos-Suarez et al., 2001; Sunnarborg et al., 2002; Sahin et al., 2004), fractalkine (Garton et al., 2001), amyloid precursor protein (Buxbaum et al., 1998), p75 neurotrophin-receptor (Weskamp et al., 2004), and MUC1 (Thathiah et al.,…”
Matrix metalloproteinases as modulators of inflammation. (2008, background): “Fractalkine can exist as a membrane-anchored adhesion molecule, and as a soluble form shed from the cell membrane by ADAM10 and ADAM 17 that functions as a chemoattractant [44,45].”