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Prepublished online as a Blood First Edition Paper on October 31, 2002; DOI 10.1182/blood-2002-07-1965.
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Blood, 15 March 2003, Vol. 101, No. 6, pp. 2115-2124
CHEMOKINES
Differential regulation of CXCR2 trafficking by Rab
GTPases
Guo-Huang Fan,
Lynne A. Lapierre,
James R. Goldenring, and
Ann Richmond
From the Department of Veterans Affairs, Nashville, and
the Departments of Cancer Biology and Surgery, Vanderbilt
University School of Medicine, Nashville, TN.
Intracellular trafficking of chemokine receptors plays an important
role in fine-tuning the functional responses of neutrophils and
lymphocytes in the inflammatory process and HIV infection. Although
many chemokine receptors internalize through clathrin-coated pits, regulation of the receptor trafficking is not fully
understood. The present study demonstrated that CXCR2 was colocalized
with transferrin and low-density lipoprotein (LDL) after agonist
treatment for different periods of time, suggesting 2 intracellular
trafficking pathways for this receptor. CXCR2 was colocalized 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 a 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 receptor recycling was inhibited by
overexpression of a dominant-negative Rab11a-S25N mutant. After
prolonged (4-hour) agonist treatment, CXCR2 exhibited significantly
increased colocalization with Rab7, which is localized in late
endosomes. The colocalization of CXCR2 with LDL and LAMP-1 suggests
that CXCR2 is targeted to lysosomes for degradation after prolonged
ligand treatment. However, the colocalization of CXCR2 with Lamp1 was
blocked by the overexpression of a dominant-negative Rab7-T22N mutant.
In cells overexpressing Rab7-T22N, CXCR2 was retained in the Rab5- and
Rab11a-positive endosomes after prolonged (4-hour) agonist treatment.
Our data suggest that the intracellular trafficking of CXCR2 is
differentially regulated by Rab proteins.
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