Role of ubiquitylation in cellular membrane transport.
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.
Staub
Olivier
O
Department of Pharmacology and Toxicology, University of Lausanne, Lausanne, Switzerland. Olivier.Staub@unil.ch
Rotin
Daniela
D
D000818:Animals; D001692:Biological Transport / Q000502:physiology; D002462:Cell Membrane / Q000378:metabolism*; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D043743:Ubiquitin-Protein Ligase Complexes / Q000378:metabolism; D014452:Ubiquitins / Q000378:metabolism*; D015003:Yeasts / Q000378:metabolism
D008565:Membrane Proteins; D014452:Ubiquitins; D043743:Ubiquitin-Protein Ligase Complexes