doi: 10.1161/01.RES.0000261939.88744.5a
© 2007 American Heart Association, Inc.
Reviews |
Seven-Transmembrane Receptors and Ubiquitination
From the Duke University Medical Center, Departments of Medicine and Cell Biology, Durham, NC.
Correspondence to Sudha K. Shenoy, Box 3821, Duke University Medical Center, Durham, NC 27710. E-mail sudha{at}receptor-biol.duke.edu
This Review is part of a thematic series on Ubiquitination, which includes the following articles:
Regulation of G Protein and Mitogen-Activated Protein Kinase Signaling by Ubiquitination: Insights From Model Organisms
Heart Failure and Protein Quality Control
Seven-Transmembrane Receptors and Ubiquitination
Ubiquitin and Ubiquitin-Like Proteins in Protein Regulation
Sudha K. Shenoy Guest Editor
Regulation of protein function by posttranslational modification plays an important role in many biological pathways. The most well known among such modifications is protein phosphorylation performed by highly specific protein kinases. In the past decade, however, covalent linkage of the low-molecular-weight protein ubiquitin to substrate proteins (protein ubiquitination) has proven to be yet another widely used mechanism of protein regulation playing a crucial role in virtually all aspects of cellular functions. This review highlights some of the recently discovered and provocative roles for ubiquitination in the regulation of the life cycle and signal transduction properties of 7-transmembrane receptors that serve to integrate many biological functions and play fundamental roles in cardiovascular homeostasis.
Key Words: GPCR • GRK • ß-arrestin • internalization • degradation
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