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Prepublished online as a Blood First Edition Paper on October 31, 2002; DOI 10.1182/blood-2002-07-1965.
Submitted July 2, 2002
Accepted October 25, 2002
Differential regulation of CXCR2 trafficking by Rab GTPases
Guo-Huang Fan, Lynne A Lapierre, James R Goldenring, and Ann Richmond*
Department of Veterans Affairs, Nashville, TN, USA; Department of Cancer Biology, Vanderbilt University, Nashville, TN, USA
Department of Surgery, Vanderbilt University, Nashville, TN, USA
* Corresponding author; email: ann.richmond{at}vanderbilt.edu.
The intracellular trafficking of chemokine receptors plays an important role in fine tuning the functional responses of neutrophils and lymphocytes in inflammatory process and HIV infection. Although many chemokine receptors internalize through clathrin-coated pits, regulations of the receptor trafficking are not fully understood. The present study demonstrated that CXCR2 was co-localized with transferrin and LDL after agonist treatment for different period of time, suggesting two intracellular trafficking pathways for this receptor. CXCR2 was co-localized with Rab5 and Rab11a, which are localized in early and recycling endosomes respectively, in response to agonist stimulation for a short period of time, suggesting recycling pathway for the receptor trafficking. However, overexpression of a dominant negative Rab5-S34N mutant significantly attenuated CXCR2 sequestration. The internalized CXCR2 was recycled back to the cell surface after removal of the agonist and recovery of the cells, but the receptor recycling was inhibited by overexpression of a dominant negative Rab11a-S25N mutant. After prolonged (4 h) agonist treatment, CXCR2 exhibited significantly increased co-localization with Rab7, which is localized in late endosomes. The co-localization of CXCR2 with LDL and LAMP-1 suggests that CXCR2 is targeted to lysosomes for degradation after prolonged ligand treatment. However, the co-localization of CXCR2 with Lamp1 was blocked by overexpression of a dominant negative Rab7-T22N mutant. In the cells overexpressing Rab7-T22N, CXCR2 was retained in the Rab5 and Rab11a positive endosomes after prolonged (4 h) agonist treatment. Our data suggest that the intracellular trafficking of CXCR2 is regulated differentially by Rab proteins.
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