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Mueller, A. 
ORCID: https://orcid.org/0000-0003-0774-0434 and Strange, P. G.
(2004)
Mechanisms of internalization and recycling of the chemokine receptor, CCR5.
European Journal of Biochemistry, 271 (2).
pp. 243-252.
ISSN 0014-2956
Abstract
CCR5 is a G protein-coupled receptor that binds several natural chemokines but it is also a coreceptor for the entry of M tropic strains of HIV-1 into cells. Levels of CCR5 on the cell surface are important for the rate of HIV-1 infection and are determined by a number of factors including the rates of CCR5 internalization and recycling. Here we investigated the involvement of the actin cytoskeleton in the control of ligand-induced internalization and recycling of CCR5. Cytochalasin D, an actin depolymerizing agent, inhibited chemokine-induced internalization of CCR5 and recycling of the receptor in stably transfected CHO cells and in the monocytic cell line, THP-1. CCR5 internalization and recycling were inhibited by Toxin B and C-3 exoenzyme treatment in CHO and THP-1 cells, confirming activation of members of the RhoGTPase family by CCR5. The specific Rho kinase inhibitor Y27632, however, had no effect on CCR5 internalization or recycling. Ligand-induced activation of CCR5 leads to Rho kinase-dependent formation of focal adhesion complexes. These data indicate that CCR5 internalization and recycling are regulated by actin polymerization and activation of small G proteins in a Rho-dependent manner.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | sdg 3 - good health and well-being ,/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_being |
| Faculty \ School: | Faculty of Science > School of Pharmacy |
| UEA Research Groups: | Faculty of Science > Research Groups > Pharmaceutical Cell Biology (former - to 2017) Faculty of Science > Research Groups > Molecular and Tissue Pharmacology |
| Depositing User: | Rachel Smith |
| Date Deposited: | 31 May 2011 14:03 |
| Last Modified: | 24 Oct 2022 02:43 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/31564 |
| DOI: | 10.1046/j.1432-1033.2003.03918.x |
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