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Prepublished online as a Blood First Edition Paper on October 31, 2002; DOI 10.1182/blood-2002-07-1965. This Article Full Text (PDF) All Versions of this Article: 2002-07-1965v1 101/6/2115    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Fan, G.-H. Articles by Richmond, A. Search for Related Content PubMed PubMed Citation Articles by Fan, G.-H. Articles by Richmond, A. Social Bookmarking                   What's this? 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. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: Y.-W. Huang, P. Su, G. Y. Liu, M. R. Crow, D. Chaukos, H. Yan, and L. A. Robinson Constitutive Endocytosis of the Chemokine CX3CL1 Prevents Its Degradation by Cell Surface Metalloproteases J. Biol. Chem., October 23, 2009; 284(43): 29644 - 29653. [Abstract] [Full Text] [PDF] B. W. Jones and P. M. Hinkle Subcellular Trafficking of the TRH Receptor: Effect of Phosphorylation Mol. Endocrinol., September 1, 2009; 23(9): 1466 - 1478. [Abstract] [Full Text] [PDF] R. Stillie, S. M. Farooq, J. R. Gordon, and A. W. Stadnyk The functional significance behind expressing two IL-8 receptor types on PMN J. Leukoc. 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