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J Biol Chem, Vol. 275, Issue 4, 2479-2485, January 28, 2000
-Arrestin Differentially Regulates the Chemokine Receptor
CXCR4-mediated Signaling and Receptor Internalization, and This
Implicates Multiple Interaction Sites between -Arrestin and
CXCR4*
From the Shanghai Institute of Cell Biology, Chinese Academy of
Sciences, Shanghai 200031, People's Republic of China
The chemokine receptor CXCR4 has recently been
shown to be a co-receptor involved in the entry of human
immunodeficiency virus type 1 into target cells. This study shows that
coexpression of 
-arrestin with CXCR4 in human embryonic kidney 293 cells attenuated chemokine-stimulated G protein activation and
inhibition of cAMP production. Truncation of the C-terminal 34 amino
acids of CXCR4 (CXCR4-T) abolished the effects of -arrestin on
CXCR4/G protein signaling, indicating the functional interaction of the
receptor C terminus with -arrestin. On the other hand, receptor
internalization and the subsequent activation of extracellular
signal-regulated kinases were significantly promoted by coexpression of
-arrestin with CXCR4, whereas the C-terminal truncation of CXCR4 did
not affect this regulation of -arrestin, suggesting that
-arrestin can functionally interact with CXCR4 with or without the C
terminus. Moreover, 2V54D, the dominant inhibitory
mutant of -arrestin 2, exerted no effects on CXCR4/G protein
signaling, but strongly influenced receptor internalization and
extracellular signal-regulated kinase activation. Further cross-linking
experiments demonstrated that -arrestin as well as
2V54D could physically contact both CXCR4 and CXCR4-T.
Glutathione S-transferase pull-down assay showed that
-arrestin was able to bind efficiently in vitro to both the third intracellular loop and the 34-amino acid C terminus of CXCR4.
Taken together, our data clearly establish that -arrestin can
effectively regulate different functions of CXCR4 and that this is
mediated through its distinct interactions with the C terminus and
other regions including the third loop of CXCR4.
To whom correspondence should be addressed: Shanghai Inst. of Cell
Biology, 320 Yue Yang Rd., Shanghai 200031, People's Republic of
China. Tel.: 21-6471-6049; Fax: 21-6471-8563; E-mail:
gangpei@sunm.shcnc.ac.cn.
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