4.6 Review

Divergent pathways lead to ESCRT-III-catalyzed membrane fission

Journal

TRENDS IN BIOCHEMICAL SCIENCES
Volume 36, Issue 4, Pages 199-210

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2010.09.004

Keywords

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Funding

  1. Agence Nationale de la Recherche [ANR-08-BLAN-0271-01]
  2. Deutsche Forschungsgemeinschaft [SPP1175]
  3. Human Frontier Science Program long-term postdoctoral fellowship
  4. Fondation pour la Recherche Medicale (FRM)
  5. Rhone-Alpes program Cluster 10 Infectiologie
  6. Agence Nationale de la Recherche (ANR) [ANR-08-BLAN-0271] Funding Source: Agence Nationale de la Recherche (ANR)

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Endosomal sorting complexes required for transport (ESCRT) have been implicated in topologically similar but diverse cellular and pathological processes including multivesicular body (MVB) biogenesis, cytokinesis and enveloped virus budding. Although receptor sorting at the endosomal membrane producing MVBs employs the regulated assembly of ESCRT-0 followed by ESCRT-I, -II, -III and the vacuolar protein sorting (VPS)4 complex, other ESCRT-catalyzed processes require only a subset of complexes which commonly includes ESCRT-III and VPS4. Recent progress has shed light on the pathway of ESCRT assembly and highlights the separation of tasks of different ESCRT complexes and associated partners. The emerging picture suggests that among all ESCRT-catalyzed processes, divergent pathways lead to ESCRT-III assembly within the neck of a budding structure catalyzing membrane fission.

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