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

PERSPECTIVES

ß-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.

*Corresponding author: E-mail: strous{at}med.uu.nl

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 ß2-adrenergic receptor (ß-AR) through interactions with ß-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.

Citation:
G. J. Strous, J. A. Schantl, ß-Arrestin and Mdm2, Unsuspected Partners in Signaling from the Cell Surface. Science's STKE (2001), http://stke.sciencemag.org/cgi/content/full/OC_sigtrans;2001/110/pe41.

© 2001 American Association for the Advancement of Science

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

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