1. ESCRT-III and Vps4: a dynamic multipurpose tool for membrane budding and scission
- Author
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David Teis, Simona M. Migliano, and Manuel Alonso Y Adell
- Subjects
0301 basic medicine ,Endosome ,Vesicular Transport Proteins ,Endosomes ,macromolecular substances ,Biology ,Exosomes ,Models, Biological ,Biochemistry ,ESCRT ,03 medical and health sciences ,Animals ,Humans ,Nuclear pore ,Molecular Biology ,Virus Release ,Cytokinesis ,Neuronal Plasticity ,Endosomal Sorting Complexes Required for Transport ,Cell Membrane ,Autophagosomes ,Cell Biology ,Membrane budding ,Transport protein ,Cell biology ,Protein Transport ,Midbody ,030104 developmental biology ,Vacuoles - Abstract
Complex molecular machineries bud, scission and repair cellular membranes. Components of the multi-subunit endosomal sorting complex required for transport (ESCRT) machinery are enlisted when multivesicular bodies are generated, extracellular vesicles are formed, the plasma membrane needs to be repaired, enveloped viruses bud out of host cells, defective nuclear pores have to be cleared, the nuclear envelope must be resealed after mitosis and for final midbody abscission during cytokinesis. While some ESCRT components are only required for specific processes, the assembly of ESCRT-III polymers on target membranes and the action of the AAA-ATPase Vps4 are mandatory for every process. In this review, we summarize the current knowledge of structural and functional features of ESCRT-III/Vps4 assemblies in the growing pantheon of ESCRT-dependent pathways. We describe specific recruitment processes for ESCRT-III to different membranes, which could be useful to selectively inhibit ESCRT function during specific processes, while not affecting other ESCRT-dependent processes. Finally, we speculate how ESCRT-III and Vps4 might function together and highlight how the characterization of their precise spatiotemporal organization will improve our understanding of ESCRT-mediated membrane budding and scission in vivo.
- Published
- 2016