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J. Biol. Chem., Vol. 279, Issue 9, 7807-7811, February 27, 2004
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-Arrestins 1 and 2*
From the
Howard Hughes Medical Institute, Department of Medicine and Biochemistry, Duke University Medical Center, Durham, North Carolina 27710
-Arrestin2 not only plays essential roles in seven membrane-spanning receptor desensitization and internalization but also functions as a signal transducer in mitogen-activated protein kinase cascades. Here we show that the angiotensin II type 1A receptor-mediated activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) in HEK-293 cells is increased when the cellular level of -arrestin1 is down-regulated by RNA interference but is decreased or eliminated when the cellular level of -arrestin2 is diminished. Such reciprocal effects of down-regulated levels of -arrestins 1 and 2 are primarily due to differences in the ability of the two forms of -arrestins to directly mediate ERK activation. These results are the first to demonstrate reciprocal activity of -arrestin isoforms on a signaling pathway and suggest that physiological levels of -arrestin1 may act as "dominant-negative" inhibitors of -arrestin2-mediated ERK activation.
Received for publication, October 8, 2003 , and in revised form, January 6, 2004.
* This work was supported by Grant RO1 HL16037 (to R. J. L.) from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
To whom correspondence should be addressed: Howard Hughes Medical Inst., Depts. of Medicine and Biochemistry, Box 3821, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-2974; Fax: 919-684-8875; E-mail: lefko001{at}receptor-biol.duke.edu.
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