CX3CR1 binds CX3CL1

Stable Identifier
Reaction [binding]
Homo sapiens
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CX3CL1 (fractalkine) is a member of the chemokine superfamily and functions as a human leukocyte chemoattractant protein (Bazan JF et al, 1997). Unlike other human chemokines, the chemokine domain of fractalkine has three amino acids between two conserved cysteines, referred to as the CX3C motif. This molecule can exist in two forms: either membrane-anchored or as a shed 95K glycoprotein. The soluble form has potent chemoattractant activity for T-cells and monocytes, and the membrane-bound protein, which is induced on activated primary endothelial cells, promotes strong adhesion of those leukocytes. The seven-transmembrane high-affinity receptor for fractalkine, termed CX3C1, mediates both the adhesive and migratory functions of fractalkine (Imai T et al, 1997). CX3CL1 is reported to signal via Gi (Brandt et al. 2002).
Literature References
PubMed ID Title Journal Year
9390561 Identification and molecular characterization of fractalkine receptor CX3CR1, which mediates both leukocyte migration and adhesion

Yoshie, O, Nishimura, M, Takagi, S, Haskell, C, Schall, TJ, Baba, M, Hieshima, K, Kakizaki, M, Nagira, M, Nomiyama, H, Imai, T

Cell 1997
9024663 A new class of membrane-bound chemokine with a CX3C motif

Greaves, DR, Soo, K, Zlotnik, A, Rossi, D, Schall, TJ, Hardiman, G, Bacon, KB, Bazan, JF, Wang, W

Nature 1997
Orthologous Events
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