Seven-transmembrane receptors and ubiquitination.
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.
Shenoy
Sudha K
SK
Duke University Medical Center, Departments of Medicine and Cell Biology, Durham, NC 27710, USA. sudha@receptor-biol.duke.edu
D000818:Animals; D006801:Humans; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D043562:Receptors, G-Protein-Coupled / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology; D025801:Ubiquitin / Q000235:genetics / Q000378:metabolism*
D043562:Receptors, G-Protein-Coupled; D025801:Ubiquitin