期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 322, 期 1, 页码 42-49出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2004.07.076
关键词
G-protein coupled receptor; endocytosis; chemokine receptor; caveolae; lipid rafts; clathrin-coated vesicles; dynamin
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 vitally encoded chemokine receptor homologue. (C) 2004 Elsevier Inc. All rights reserved.
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