Beta-arrestin and Mdm2, unsuspected partners in signaling from the cell surface.
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 beta(2)-adrenergic receptor (beta-AR) through interactions with beta-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.
Strous
G J
GJ
University Medical Center Utrecht, Department of Cell Biology, 3584-CX Utrecht, Netherlands. strous@med.uu.nl
Schantl
J A
JA
D000818:Animals; D019390:Arrestins / Q000502:physiology*; D002352:Carrier Proteins / Q000502:physiology*; D002462:Cell Membrane / Q000502:physiology; D006801:Humans; D008025:Ligases / Q000502:physiology; D009687:Nuclear Proteins; D011518:Proto-Oncogene Proteins / Q000502:physiology*; D051736:Proto-Oncogene Proteins c-mdm2; D015398:Signal Transduction / Q000502:physiology*; D044767:Ubiquitin-Protein Ligases; D000071557:beta-Arrestins
D019390:Arrestins; D002352:Carrier Proteins; D009687:Nuclear Proteins; D011518:Proto-Oncogene Proteins; D000071557:beta-Arrestins; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2; D044767:Ubiquitin-Protein Ligases; D008025:Ligases