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Papers In Press, published online ahead of print May 17, 2004
Center for Immunology and Inflammatory Diseases, Division of Rheumatology, Allergy and Immunology, Massachusetts General Hospital, Charlestown, MA 02129
Corresponding Author: aluster{at}partners.org
The chemokine receptor CXCR3 is a G protein-coupled receptor found predominantly on T cells that is activated by 3 ligands: CXCL9 (Mig), CXCL10 (IP-10), and CXCL11 (I-TAC). Previously, we have found that of the three ligands, CXCL11 is the most potent inducer of CXCR3 internalization and is the physiologic inducer of CXCR3 internalization after T cell contact with activated endothelial cells. We have therefore hypothesized that these three ligands transduce different signals to CXCR3. In light of this hypothesis, we sought to determine if regions of CXCR3 are differentially required for CXCL9, CXCL10, and CXCL11 function. Here we identified two distinct domains that contributed to CXCR3 internalization. The carboxyl-terminal domain and ß-arrestin1 were predominantly required by CXCL9 and CXCL10, and the third intracellular loop was predominantly required by CXCL11. Chemotaxis and calcium mobilization induced by all three CXCR3 ligands were dependent on the CXCR3 carboxyl-terminus and the DRY sequence in the third trans-membrane domain. Our findings demonstrate that distinct domains of CXCR3 mediate its functions and suggest that the differential requirement of these domains contributes to the complexity of the chemokine system.
J. Biol. Chem, 10.1074/jbc.M403595200
Submitted on March 31, 2004
Revised on May 7, 2004
Accepted on May 17, 2004
Intracellular domains of CXCR3 that mediate CXCL9, CXCL10, and CXCL11 function
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