Helmholtz Gemeinschaft


HCMV-encoded chemokine receptor US28 employs multiple routes for internalization

Item Type:Article
Title:HCMV-encoded chemokine receptor US28 employs multiple routes for internalization
Creators Name:Droese, J. and Mokros, T. and Hermosilla, R. and Schuelein, R. and Lipp, M. and Höpken, U.E. and Rehm, A.
Abstract:The human cytomegalovirus-encoded G protein-coupled receptor homologue US28 binds inflammatory chemokines and sequesters them from the environment of infected cells. Low surface deposition and endocytosis are dependent on constitutive C-terminal phosphorylation, suggesting a requirement for {beta}-arrestin binding in receptor internalization. In this report, a US28-dependent redistribution of {beta}-arrestin into vesicular structures occurred, although internalization of US28 was independent of {beta}-arrestin. Internalization of US28 was dynamin-dependent, and US28 partially partitioned into the detergent-resistant membrane fraction. Endocytosis was diminished by cholesterol depletion, yet sucrose inhibition was even stronger. The relevance of the clathrin-coated pit pathway was supported by colocalization of {beta} 2-adaptin and US28 in endocytic compartments. Exchange of the C-terminal dileucine endocytosis motif inhibited rapid endocytosis, indicating a direct interaction of US28 with the AP-2 adaptor complex. We suggest that the arrestin-independent, dynamin-dependent internalization of US28 reveals a differential sorting of {beta}-arrestins and the virally encoded chemokine receptor homologue.
Keywords:Caveolae, Chemokine Receptor, Clathrin-Coated Vesicles, Dynamin, Endocytosis, G-protein Coupled Receptor, Lipid Rafts
Source:Biochemical and Biophysical Research Communications
Publisher:Academic Press
Page Range:42-49
Date:10 September 2004
Official Publication:https://doi.org/10.1016/j.bbrc.2004.07.076
PubMed:View item in PubMed

Repository Staff Only: item control page

Open Access
MDC Library