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Department of Pharmacology and Toxicology, University of Lausanne, Lausanne, Switzerland; and Program in Cell Biology, The Hospital for Sick Children, and Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada
Ubiquitylation of membrane proteins has gained considerable interest in recent years. It has been recognized as a signal that negatively regulates the cell surface expression of many plasma membrane proteins both in yeast and in mammalian cells. Moreover, it is also involved in endoplasmic reticulum-associated degradation of membrane proteins, and it acts as a sorting signal both in the secretory pathway and in endosomes, where it targets proteins into multivesicular bodies in the lumen of vacuoles/lysosomes. In this review we discuss the progress in understanding these processes, achieved during the past several years.
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