Abstract
The endosomal-sorting complex required for transport (ESCRT) apparatus has multiple ubiquitin (Ub)-binding domains and participates in a wide variety of cellular processes. Many of these ESCRT-dependent processes are keenly regulated by Ub, which serves as a lysosomal-sorting signal for membrane proteins targeted into multivesicular bodies (MVBs) and which may serve as a mediator of viral budding from the cell surface. Hints that both ESCRTs and Ub work together in the processes such as cytokinesis, transcription and autophagy are beginning to emerge. Here, we explore the relationship between ESCRTs and Ub in MVB sorting and viral budding.
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