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Sci. STKE, 27 November 2001
Vol. 2001, Issue 110, p. pe41
[DOI: 10.1126/stke.2001.110.pe41]


β-Arrestin and Mdm2, Unsuspected Partners in Signaling from the Cell Surface

Ger J. Strous* and Julia A. Schantl

University Medical Center Utrecht, Department of Cell Biology, 3584-CX Utrecht, Netherlands.

Abstract: Mdm2 is a ubiquitin-protein ligase known to ubiquitinate p53, promoting its degradation by the ubiquitin-proteasome system. Shenoy and co-workers showed that Mdm2 can act as a key factor in the sequestration of the cell surface β2-adrenergic receptor (β-AR) through interactions with β-arrestin. Strous and Schantl discuss how Mdm2 may be a switch connecting extracellular signals mediated through G protein-coupled receptors (GPCRs) to p53 and its functions in apoptosis and cell cycle progression.

*Corresponding author: E-mail: strous{at}

Citation: G. J. Strous, J. A. Schantl, β-Arrestin and Mdm2, Unsuspected Partners in Signaling from the Cell Surface. Sci. STKE 2001, pe41 (2001).

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